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Conserved domains on  [gi|568996333|ref|XP_006522671|]
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ankyrin repeat and SAM domain-containing protein 3 isoform X1 [Mus musculus]

Protein Classification

ankyrin repeat domain-containing protein( domain architecture ID 12789526)

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];
39-221 1.51e-47

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 169.75  E-value: 1.51e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996333  39 LHTAASIGQHEVVKECVQRGeLDLNKKNGGGWTALMYASYIGHDTIVHLLLEAGVSVNVPTPEGQTPLMLASSCGNESIA 118
Cdd:COG0666   91 LHAAARNGDLEIVKLLLEAG-ADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIV 169

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996333 119 YFLLQQGAELEMKDIHGWTALFHCTSAGHQQMVKFLLESGANANVREPvYGYTPLMEAAASGHEIIVQYFLNHGVKVDTR 198
Cdd:COG0666  170 KLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDN-DGKTALDLAAENGNLEIVKLLLEAGADLNAK 248

                        170       180
                 ....*....|....*....|...
gi 568996333 199 DHSGATACMLARQFGHMKIVALM 221
Cdd:COG0666  249 DKDGLTALLLAAAAGAALIVKLL 271
SAM_ANKS3 cd09519
SAM domain of ANKS3 subfamily; SAM (sterile alpha motif) domain of ANKS3 subfamily is a ...
 423-486 3.35e-37

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: 133.00  E-value: 3.35e-37
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568996333 423 YSGPQDLATLLEQIGCLKYLQVFEEQDIDLRIFLTLTESDLKEIGITLFGPKRKMTSAIARWHS 486
Cdd:cd09519    1 YTGPKDLSELLEQIGCSKYLPIFEEQDIDLRIFLTLTESDLKEIGITLFGPKRKMTSAIARWHS 64
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
39-221 1.51e-47

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 169.75  E-value: 1.51e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996333  39 LHTAASIGQHEVVKECVQRGeLDLNKKNGGGWTALMYASYIGHDTIVHLLLEAGVSVNVPTPEGQTPLMLASSCGNESIA 118
Cdd:COG0666   91 LHAAARNGDLEIVKLLLEAG-ADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIV 169

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996333 119 YFLLQQGAELEMKDIHGWTALFHCTSAGHQQMVKFLLESGANANVREPvYGYTPLMEAAASGHEIIVQYFLNHGVKVDTR 198
Cdd:COG0666  170 KLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDN-DGKTALDLAAENGNLEIVKLLLEAGADLNAK 248

                        170       180
                 ....*....|....*....|...
gi 568996333 199 DHSGATACMLARQFGHMKIVALM 221
Cdd:COG0666  249 DKDGLTALLLAAAAGAALIVKLL 271
SAM_ANKS3 cd09519
SAM domain of ANKS3 subfamily; SAM (sterile alpha motif) domain of ANKS3 subfamily is a ...
 423-486 3.35e-37

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: 133.00  E-value: 3.35e-37
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568996333 423 YSGPQDLATLLEQIGCLKYLQVFEEQDIDLRIFLTLTESDLKEIGITLFGPKRKMTSAIARWHS 486
Cdd:cd09519    1 YTGPKDLSELLEQIGCSKYLPIFEEQDIDLRIFLTLTESDLKEIGITLFGPKRKMTSAIARWHS 64
Ank_2 pfam12796
Ankyrin repeats (3 copies);
106-199 9.24e-23

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.87  E-value: 9.24e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996333  106 LMLASSCGNESIAYFLLQQGAELEMKDIHGWTALFHCTSAGHQQMVKFLLEsgaNANVREPVYGYTPLMEAAASGHEIIV 185
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE---HADVNLKDNGRTALHYAARSGHLEIV 77

                          90
                  ....*....|....
gi 568996333  186 QYFLNHGVKVDTRD 199
Cdd:pfam12796  78 KLLLEKGADINVKD 91
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 73-246 1.46e-15

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 80.68  E-value: 1.46e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996333  73 LMYASYIGHDTIVHLLLEAGVSVNVPTPEGQTPLMLASSCGNESIAYFLLQQGAELEMKDIHGWTALFHCTSAGHQQMVK 152
Cdd:PLN03192 529 LLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFR 608

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996333 153 FLLESganANVREPVYGYTPLMEAAASGHEIIVQYFLNHGVKVDTRDHSGATACMLARQFGHMKIVALMETHSPVLPKSl 232
Cdd:PLN03192 609 ILYHF---ASISDPHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKA- 684

                        170
                 ....*....|....
gi 568996333 233 yrspEKYEDLSSSD 246
Cdd:PLN03192 685 ----NTDDDFSPTE 694
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 423-484 4.13e-11

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: 58.82  E-value: 4.13e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568996333  423 YSGPQDLATLLEQIGCLKYLQVFEEQDIDLRIFLTLTESDLKEIGITLFGPKRKMTSAIARW 484
Cdd:pfam00536   2 GWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLKLGVTLLGHRKKILYAIQRL 63
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 422-481 3.65e-10

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.


Pssm-ID: 197735  Cd Length: 68  Bit Score: 56.15  E-value: 3.65e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568996333   422 PYSGPQDLATLLEQIGCLKYLQVFEEQDIDLRIFLTLT-ESDLKEIGITLFGPKRKMTSAI 481
Cdd:smart00454   2 SQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTsEEDLKELGITKLGHRKKILKAI 62
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 168-196 1.41e-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: 39.49  E-value: 1.41e-04
                           10        20
                   ....*....|....*....|....*....
gi 568996333   168 YGYTPLMEAAASGHEIIVQYFLNHGVKVD 196
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 69-190 6.06e-04

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 43.08  E-value: 6.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996333  69 GWTALMYASYIGHDTIVHLLLEAGVSVNVPTPEG--------------QTPLMLASSCGNESIAYFLLQQGAELEMKDIH 134
Cdd:cd22192   89 GETALHIAVVNQNLNLVRELIARGADVVSPRATGtffrpgpknliyygEHPLSFAACVGNEEIVRLLIEHGADIRAQDSL 168

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568996333 135 GWTALFHCTSAGHQ----QMVKFLLESGANANvREPVY------GYTPLMEAAASGHEIIVQYFLN 190
Cdd:cd22192  169 GNTVLHILVLQPNKtfacQMYDLILSYDKEDD-LQPLDlvpnnqGLTPFKLAAKEGNIVMFQHLVQ 233
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 39-139 3.49e-03

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 40.83  E-value: 3.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996333   39 LHtAASIGQHEVVKECVQRgELDLNKKNGGGW--------------TALMYASYIGHDTIVHLLLEAGVSVN-------- 96
Cdd:TIGR00870  86 LH-AISLEYVDAVEAILLH-LLAAFRKSGPLElandqytseftpgiTALHLAAHRQNYEIVKLLLERGASVParacgdff 163

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 568996333   97 VPTPE------GQTPLMLASSCGNESIAYFLLQQGAELEMKDIHGWTAL 139
Cdd:TIGR00870 164 VKSQGvdsfyhGESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLL 212
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
39-221 1.51e-47

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 169.75  E-value: 1.51e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996333  39 LHTAASIGQHEVVKECVQRGeLDLNKKNGGGWTALMYASYIGHDTIVHLLLEAGVSVNVPTPEGQTPLMLASSCGNESIA 118
Cdd:COG0666   91 LHAAARNGDLEIVKLLLEAG-ADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIV 169

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996333 119 YFLLQQGAELEMKDIHGWTALFHCTSAGHQQMVKFLLESGANANVREPvYGYTPLMEAAASGHEIIVQYFLNHGVKVDTR 198
Cdd:COG0666  170 KLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDN-DGKTALDLAAENGNLEIVKLLLEAGADLNAK 248

                        170       180
                 ....*....|....*....|...
gi 568996333 199 DHSGATACMLARQFGHMKIVALM 221
Cdd:COG0666  249 DKDGLTALLLAAAAGAALIVKLL 271
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
38-224 4.27e-47

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 168.21  E-value: 4.27e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996333  38 DLHTAASIGQHEVVKECVQRGELDLNKKNGGGWTALMYASYIGHDTIVHLLLEAGVSVNVPTPEGQTPLMLASSCGNESI 117
Cdd:COG0666   56 LLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEI 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996333 118 AYFLLQQGAELEMKDIHGWTALFHCTSAGHQQMVKFLLESGANANVREPvYGYTPLMEAAASGHEIIVQYFLNHGVKVDT 197
Cdd:COG0666  136 VKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDN-DGETPLHLAAENGHLEIVKLLLEAGADVNA 214

                        170       180
                 ....*....|....*....|....*..
gi 568996333 198 RDHSGATACMLARQFGHMKIVALMETH 224
Cdd:COG0666  215 KDNDGKTALDLAAENGNLEIVKLLLEA 241
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
39-220 6.54e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 142.79  E-value: 6.54e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996333  39 LHTAASIGQHEVVKECVQRGELDLNKKNGGGWTALMYASYIGHDTIVHLLLEAGVSVNVPTPEGQTPLMLASSCGNESIA 118
Cdd:COG0666   24 LLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIV 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996333 119 YFLLQQGAELEMKDIHGWTALFHCTSAGHQQMVKFLLESGANANVREPvYGYTPLMEAAASGHEIIVQYFLNHGVKVDTR 198
Cdd:COG0666  104 KLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDN-DGNTPLHLAAANGNLEIVKLLLEAGADVNAR 182

                        170       180
                 ....*....|....*....|..
gi 568996333 199 DHSGATACMLARQFGHMKIVAL 220
Cdd:COG0666  183 DNDGETPLHLAAENGHLEIVKL 204
SAM_ANKS3 cd09519
SAM domain of ANKS3 subfamily; SAM (sterile alpha motif) domain of ANKS3 subfamily is a ...
 423-486 3.35e-37

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: 133.00  E-value: 3.35e-37
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568996333 423 YSGPQDLATLLEQIGCLKYLQVFEEQDIDLRIFLTLTESDLKEIGITLFGPKRKMTSAIARWHS 486
Cdd:cd09519    1 YTGPKDLSELLEQIGCSKYLPIFEEQDIDLRIFLTLTESDLKEIGITLFGPKRKMTSAIARWHS 64
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
39-205 2.68e-35

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 135.47  E-value: 2.68e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996333  39 LHTAASIGQHEVVKECVQRGeLDLNKKNGGGWTALMYASYIGHDTIVHLLLEAGVSVNVPTPEGQTPLMLASSCGNESIA 118
Cdd:COG0666  124 LHLAAYNGNLEIVKLLLEAG-ADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIV 202

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996333 119 YFLLQQGAELEMKDIHGWTALFHCTSAGHQQMVKFLLESGANANVREPvYGYTPLMEAAASGHEIIVQYFLNHGVKVDTR 198
Cdd:COG0666  203 KLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDK-DGLTALLLAAAAGAALIVKLLLLALLLLAAA 281


                 ....*..
gi 568996333 199 DHSGATA 205
Cdd:COG0666  282 LLDLLTL 288
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
60-221 3.29e-25

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 106.19  E-value: 3.29e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996333  60 LDLNKKNGGGWTALMYASYIGHDTIVHLLLEAGVSVNVPTPEGQTPLMLASSCGNESIAYFLLQQGAELEMKDIHGWTAL 139
Cdd:COG0666   12 LAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLL 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996333 140 FHCTSAGHQQMVKFLLESGANANVREPvYGYTPLMEAAASGHEIIVQYFLNHGVKVDTRDHSGATACMLARQFGHMKIVA 219
Cdd:COG0666   92 HAAARNGDLEIVKLLLEAGADVNARDK-DGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170


                 ..
gi 568996333 220 LM 221
Cdd:COG0666  171 LL 172
Ank_2 pfam12796
Ankyrin repeats (3 copies);
106-199 9.24e-23

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.87  E-value: 9.24e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996333  106 LMLASSCGNESIAYFLLQQGAELEMKDIHGWTALFHCTSAGHQQMVKFLLEsgaNANVREPVYGYTPLMEAAASGHEIIV 185
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE---HADVNLKDNGRTALHYAARSGHLEIV 77

                          90
                  ....*....|....
gi 568996333  186 QYFLNHGVKVDTRD 199
Cdd:pfam12796  78 KLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
73-164 1.34e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.49  E-value: 1.34e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996333   73 LMYASYIGHDTIVHLLLEAGVSVNVPTPEGQTPLMLASSCGNESIAYFLLQQgAELEMKDiHGWTALFHCTSAGHQQMVK 152
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|..
gi 568996333  153 FLLESGANANVR 164
Cdd:pfam12796  79 LLLEKGADINVK 90
SAM_BICC1 cd09520
SAM domain of BICC1 (bicaudal) subfamily; SAM (sterile alpha motif) domain of BICC1 (bicaudal) ...
 423-482 2.96e-18

SAM domain of BICC1 (bicaudal) subfamily; SAM (sterile alpha motif) domain of BICC1 (bicaudal) subfamily is a protein-protein interaction domain. Proteins of this group have N-terminal K homology RNA-binding vigilin-like repeats and a C-terminal SAM domain. BICC1 is involved in the regulation of embryonic differentiation. It plays a role in the regulation of Dvl (Dishevelled) signaling, particularly in the correct cilia orientation and nodal flow generation. In Drosophila, disruption of BICC1 can disturb the normal migration direction of the anterior follicle cell of oocytes; the specific function of SAM is to recruit whole protein to the periphery of P-bodies. In mammals, mutations in this gene are associated with polycystic kidney disease and it was suggested that the BICC1 protein can indirectly interact with ANKS6 protein (ANKS6 is also associated with polycystic kidney disease) through some protein and RNA intermediates.


Pssm-ID: 188919  Cd Length: 65  Bit Score: 79.26  E-value: 2.96e-18
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996333 423 YSGPQDLATLLEQIGCLKYLQVFEEQDIDLRIFLTLTESDLKEIGITLFGPKRKMTSAIA 482
Cdd:cd09520    1 SAKYSDLPELLAKLGLEKYIDLFAQQEIDLQTFLTLTDQDLKELGITAFGARRKMLLAIS 60
Ank_2 pfam12796
Ankyrin repeats (3 copies);
39-132 1.59e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 77.85  E-value: 1.59e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996333   39 LHTAASIGQHEVVKECVQRGElDLNKKNGGGWTALMYASYIGHDTIVHLLLEaGVSVNVpTPEGQTPLMLASSCGNESIA 118
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGA-DANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNL-KDNGRTALHYAARSGHLEIV 77

                          90
                  ....*....|....
gi 568996333  119 YFLLQQGAELEMKD 132
Cdd:pfam12796  78 KLLLEKGADINVKD 91
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 73-246 1.46e-15

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 80.68  E-value: 1.46e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996333  73 LMYASYIGHDTIVHLLLEAGVSVNVPTPEGQTPLMLASSCGNESIAYFLLQQGAELEMKDIHGWTALFHCTSAGHQQMVK 152
Cdd:PLN03192 529 LLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFR 608

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996333 153 FLLESganANVREPVYGYTPLMEAAASGHEIIVQYFLNHGVKVDTRDHSGATACMLARQFGHMKIVALMETHSPVLPKSl 232
Cdd:PLN03192 609 ILYHF---ASISDPHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKA- 684

                        170
                 ....*....|....
gi 568996333 233 yrspEKYEDLSSSD 246
Cdd:PLN03192 685 ----NTDDDFSPTE 694
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 49-197 6.08e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 74.32  E-value: 6.08e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996333  49 EVVKECVQRGElDLNKKNGGGWTALMYASY--IGHDTIVHLLLEAGVSVNVPTPEGQTPLMLASSCGNE--SIAYFLLQQ 124
Cdd:PHA03100  87 EIVKLLLEYGA-NVNAPDNNGITPLLYAISkkSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDK 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996333 125 GA------ELEM----------KDIHGWTALFHCTSAGHQQMVKFLLESGANANVREpVYGYTPLMEAAASGHEIIVQYF 188
Cdd:PHA03100 166 GVdinaknRVNYllsygvpiniKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVN-KYGDTPLHIAILNNNKEIFKLL 244


                 ....*....
gi 568996333 189 LNHGVKVDT 197
Cdd:PHA03100 245 LNNGPSIKT 253
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 428-483 9.77e-14

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: 66.11  E-value: 9.77e-14
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 568996333 428 DLATLLEQIGCLKYLQVFEEQDIDLRIFLTLTESDLKEIGITLFGPKRKMTSAIAR 483
Cdd:cd09487    1 DVAEWLESLGLEQYADLFRKNEIDGDALLLLTDEDLKELGITSPGHRKKILRAIQR 56
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
84-220 1.14e-12

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 69.21  E-value: 1.14e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996333  84 IVHLLLEAGVSVNVPTPEGQTPLMLASSCGNESIAYFLLQQGAELEMKDIHGWTALFHCTSAGHQQMVKFLLESGANANV 163
Cdd:COG0666    3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568996333 164 REPvYGYTPLMEAAASGHEIIVQYFLNHGVKVDTRDHSGATACMLARQFGHMKIVAL 220
Cdd:COG0666   83 KDD-GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKL 138
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 25-204 2.07e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 69.61  E-value: 2.07e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996333  25 GAQGSPEELDVPLDLHTAASIGQHEVVKECVQRGeLDlnkkngggwTALMYASYIGHDTIvHLLLEAGVSVNVPTPEGQT 104
Cdd:PHA02874  58 GADINHINTKIPHPLLTAIKIGAHDIIKLLIDNG-VD---------TSILPIPCIEKDMI-KTILDCGIDVNIKDAELKT 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996333 105 PLMLASSCGNESIAYFLLQQGAELEMKDIHGWTALFHCTSAGHQQMVKFLLESGANANVREpVYGYTPLMEAAASGHEII 184
Cdd:PHA02874 127 FLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKD-NNGESPLHNAAEYGDYAC 205

                        170       180
                 ....*....|....*....|
gi 568996333 185 VQYFLNHGVKVDTRDHSGAT 204
Cdd:PHA02874 206 IKLLIDHGNHIMNKCKNGFT 225
PHA03095 PHA03095
ankyrin-like protein; Provisional
 49-205 1.02e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 67.74  E-value: 1.02e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996333  49 EVVKECVQRGElDLNKKNGGGWTAL-MYASYIGHDT--IVHLLLEAGVSVNVPTPEGQTPLMLASSCGN-ESIAYFLLQQ 124
Cdd:PHA03095  28 EEVRRLLAAGA-DVNFRGEYGKTPLhLYLHYSSEKVkdIVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKA 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996333 125 GAELEMKDIHGWTAL-FHCTS-AGHQQMVKFLLESGANANVREpVYGYTPLmEAAASGHEI---IVQYFLNHGVKVDTRD 199
Cdd:PHA03095 107 GADVNAKDKVGRTPLhVYLSGfNINPKVIRLLLRKGADVNALD-LYGMTPL-AVLLKSRNAnveLLRLLIDAGADVYAVD 184


                 ....*.
gi 568996333 200 HSGATA 205
Cdd:PHA03095 185 DRFRSL 190
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 61-204 1.54e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 67.00  E-value: 1.54e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996333  61 DLNKKNGGGWTALMYASYIGHDT-----IVHLLLEAGVSVNVPTPEGQTPLMLASSC--GNESIAYFLLQQGAELEMKDI 133
Cdd:PHA03100  60 DINSSTKNNSTPLHYLSNIKYNLtdvkeIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNS 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996333 134 HGWTALFHCTSAGHQ--QMVKFLLESGANANVREPV---------------YGYTPLMEAAASGHEIIVQYFLNHGVKVD 196
Cdd:PHA03100 140 DGENLLHLYLESNKIdlKILKLLIDKGVDINAKNRVnyllsygvpinikdvYGFTPLHYAVYNNNPEFVKYLLDLGANPN 219


                 ....*...
gi 568996333 197 TRDHSGAT 204
Cdd:PHA03100 220 LVNKYGDT 227
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 423-484 4.13e-11

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: 58.82  E-value: 4.13e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568996333  423 YSGPQDLATLLEQIGCLKYLQVFEEQDIDLRIFLTLTESDLKEIGITLFGPKRKMTSAIARW 484
Cdd:pfam00536   2 GWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLKLGVTLLGHRKKILYAIQRL 63
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
39-139 5.96e-11

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 63.82  E-value: 5.96e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996333  39 LHTAASIGQHEVVKECVQRGeLDLNKKNGGGWTALMYASYIGHDTIVHLLLEAGVSVNVPTPEGQTPLMLASSCGNESIA 118
Cdd:COG0666  190 LHLAAENGHLEIVKLLLEAG-ADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIV 268

                         90       100
                 ....*....|....*....|.
gi 568996333 119 YFLLQQGAELEMKDIHGWTAL 139
Cdd:COG0666  269 KLLLLALLLLAAALLDLLTLL 289
SAM_ANKS6 cd09518
SAM domain of ANKS6 (or SamCystin) subfamily; SAM (sterile alpha motif) domain of ANKS6 (or ...
 428-486 2.25e-10

SAM domain of ANKS6 (or SamCystin) subfamily; SAM (sterile alpha motif) domain of ANKS6 (or SamCystin) subfamily is a potential protein-protein interaction domain. Proteins of this subfamily have N-terminal ankyrin repeats and a C-terminal SAM domain. They are able to form self-associated complexes and both (SAM and ANK) domains play a role in such interactions. Mutations in Anks6 gene are associated with polycystic kidney disease. They cause formation of renal cysts in rodent models. It was suggested that the ANKS6 protein can interact indirectly (through RNA and protein intermediates) with BICC1, another polycystic kidney disease-associated protein.


Pssm-ID: 188917  Cd Length: 65  Bit Score: 56.81  E-value: 2.25e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 568996333 428 DLATLLEQIGCLKYLQVFEEQDIDLRIFLTLTESDLKEIGITLFGPKRKMTSAIARWHS 486
Cdd:cd09518    7 ELSGILRKLSLEKYQPIFEEQEVDMEAFLTLTDGDLKELGIKTDGPRQQILAAISELNA 65
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 422-481 3.65e-10

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.


Pssm-ID: 197735  Cd Length: 68  Bit Score: 56.15  E-value: 3.65e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568996333   422 PYSGPQDLATLLEQIGCLKYLQVFEEQDIDLRIFLTLT-ESDLKEIGITLFGPKRKMTSAI 481
Cdd:smart00454   2 SQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTsEEDLKELGITKLGHRKKILKAI 62
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 84-218 1.39e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 60.83  E-value: 1.39e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996333  84 IVHLLLEAGVSVNVPTPEGQTPLMLASSCG-----NESIAYFLLQQGAELEMKDIHGWTALFHC--TSAGHQQMVKFLLE 156
Cdd:PHA03100  50 VVKILLDNGADINSSTKNNSTPLHYLSNIKynltdVKEIVKLLLEYGANVNAPDNNGITPLLYAisKKSNSYSIVEYLLD 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996333 157 SGANANVREPvYGYTPLMEAAASGH---EII---------------VQYFLNHGVKVDTRDHSGATACMLARQFGHMKIV 218
Cdd:PHA03100 130 NGANVNIKNS-DGENLLHLYLESNKidlKILkllidkgvdinaknrVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFV 208
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
422-481 3.84e-09

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 53.43  E-value: 3.84e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568996333  422 PYSGPQDLATLLEQIGCLKYLQVFEEQDID-LRIFLTLTESDLKEIGITLFGPKRKMTSAI 481
Cdd:pfam07647   2 ESWSLESVADWLRSIGLEQYTDNFRDQGITgAELLLRLTLEDLKRLGITSVGHRRKILKKI 62
SAM_sec23ip-like cd09516
SAM domain of sec23ip-like subfamily; SAM (sterile alpha motif) domain of Sec23ip-like (Sec23 ...
 426-477 5.45e-09

SAM domain of sec23ip-like subfamily; SAM (sterile alpha motif) domain of Sec23ip-like (Sec23 interacting protein) subfamily is a potential protein-protein interaction domain. This group of proteins includes Sec23ip and DDHD2 proteins. All of them contain at least two domains: a SAM domain and a predicted metal-binding domain. For mammalian DDHD2 members of this group, phospholipase activity has been demonstrated. Sec23ip proteins of this group interact with Sec23 proteins via an N-terminal proline-rich region. Members of this subfamily are involved in organization of ER/Golgi intermediate compartment.


Pssm-ID: 188915  Cd Length: 69  Bit Score: 52.80  E-value: 5.45e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568996333 426 PQDLATLLEQIGCLKYLQVFEEQDIDLRIFLTLTESDLKEIGITLfGPKRKM 477
Cdd:cd09516    9 PLTLEEDLEKLGLSEYFDTFEKEKIDMESLLLCSESDLKEMGIPM-GPRKKL 59
Ank_4 pfam13637
Ankyrin repeats (many copies);
135-189 9.36e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.89  E-value: 9.36e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 568996333  135 GWTALFHCTSAGHQQMVKFLLESGANANVRePVYGYTPLMEAAASGHEIIVQYFL 189
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAV-DGNGETALHFAASNGNVEVLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 34-173 1.56e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 57.58  E-value: 1.56e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996333  34 DVPLDLHTAASIGQHEVVKECVQRGElDLNKKN-GGGWTALMYASYIGHDTIVHLLLEAGVSVNVPTPEGQTPLMLASSC 112
Cdd:PHA02878 133 LVYIDKKSKDDIIEAEITKLLLSYGA-DINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKH 211

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568996333 113 GNESIAYFLLQQGAELEMKDIHGWTAL-FHCTSAGHQQMVKFLLESGANANVREPVYGYTPL 173
Cdd:PHA02878 212 YNKPIVHILLENGASTDARDKCGNTPLhISVGYCKDYDILKLLLEHGVDVNAKSYILGLTAL 273
Ank_5 pfam13857
Ankyrin repeats (many copies);
55-109 1.93e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 50.81  E-value: 1.93e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 568996333   55 VQRGELDLNKKNGGGWTALMYASYIGHDTIVHLLLEAGVSVNVPTPEGQTPLMLA 109
Cdd:pfam13857   2 LEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
SAM_USH1G_HARP cd09517
SAM domain of USH1G_HARP family; SAM (sterile alpha motif) domain of USH1G/HARP (Usher ...
 429-483 1.14e-07

SAM domain of USH1G_HARP family; SAM (sterile alpha motif) domain of USH1G/HARP (Usher syndrome type-1G/ Harmonin-interacting Ankyrin Repeat-containing protein) family is a protein-protein interaction domain. Members of this family have an N-terminal ankyrin repeat region and a C-terminal SAM domain. In mammals these proteins can interact via the SAM domain with the PDZ domain of harmonin to form a scaffolding complex that facilitates signal transduction in epithelial and inner ear sensory cells. It was suggested that USH1G and HARP can be tissue specific partners of harmonin. Mutations in ush1g genes lead to Usher syndrome type 1G. This syndrome is the cause of deaf-blindness in humans.


Pssm-ID: 188916  Cd Length: 66  Bit Score: 49.26  E-value: 1.14e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568996333 429 LATLLEQIGCLKYLQVFEEQDIDLRIFLTLTESDLKEIGITLfGPKRKMTSAIAR 483
Cdd:cd09517    5 LERFLTSNHLEEYLPVFEREKIDLEALMLLTDEDLQSLKLPL-GPRRKLLNAIAK 58
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 34-192 1.37e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 54.23  E-value: 1.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996333  34 DVPLDLHTAASIGQHEVVKECVQRGEL--DLNKKNGGgwTALMYASYIGHDTIVHLLLEAGVSVNVPTPEGQTPLMLASS 111
Cdd:PHA02875  67 DIESELHDAVEEGDVKAVEELLDLGKFadDVFYKDGM--TPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVM 144

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996333 112 CGNESIAYFLLQQGAELEMKDIHGWTALFHCTSAGHQQMVKFLLESGANANVREPVYGYTPLMEAAASGHEIIVQYFLNH 191
Cdd:PHA02875 145 MGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIDIVRLFIKR 224


                 .
gi 568996333 192 G 192
Cdd:PHA02875 225 G 225
Ank_4 pfam13637
Ankyrin repeats (many copies);
69-122 2.83e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 47.65  E-value: 2.83e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 568996333   69 GWTALMYASYIGHDTIVHLLLEAGVSVNVPTPEGQTPLMLASSCGNESIAYFLL 122
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 85-221 3.51e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 53.07  E-value: 3.51e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996333  85 VHLLLEAGVSVN-VPTPEGQTPLMLASSCGNESIAYFLLQQGAELEMKDIHGWTALFHCTSAGHQQMVKFLLESGANANV 163
Cdd:PHA02875  84 VEELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDI 163

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 568996333 164 rEPVYGYTPLMEAAASGHEIIVQYFLNHGVKVDTRDHSGATACM-LARQFGHMKIVALM 221
Cdd:PHA02875 164 -EDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALcYAIENNKIDIVRLF 221
PHA03095 PHA03095
ankyrin-like protein; Provisional
 61-227 3.90e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 53.10  E-value: 3.90e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996333  61 DLNKKNGGGWTALMYasYIGHDT---IVHLLLEAGVSVNVPTPEGQTPL--MLASSCGNESIAYFLLQQGAELEMKDIHG 135
Cdd:PHA03095  75 DVNAPERCGFTPLHL--YLYNATtldVIKLLIKAGADVNAKDKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYG 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996333 136 WTALF------------------------------------HCTS-------------AGHQQM---------------- 150
Cdd:PHA03095 153 MTPLAvllksrnanvellrllidagadvyavddrfrsllhhHLQSfkprarivrelirAGCDPAatdmlgntplhsmatg 232

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996333 151 -------VKFLLESGANANVREpVYGYTPLMEAAASGHEIIVQYFLNHGVKVDTRDHSGATACMLARQFGHMKIV-ALME 222
Cdd:PHA03095 233 ssckrslVLPLLIAGISINARN-RYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVrAALA 311


                 ....*
gi 568996333 223 THSPV 227
Cdd:PHA03095 312 KNPSA 316
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 29-225 4.27e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 53.04  E-value: 4.27e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996333  29 SPEELDVPLDlhTAASIGQHEVVKECVQRGElDLNKKNGGGWTALMYASYIGHDTIVHLLLEAGVSVNV-PTPegqtplm 107
Cdd:PHA02874  31 SVDETTTPLI--DAIRSGDAKIVELFIKHGA-DINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSIlPIP------- 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996333 108 lassCGNESIAYFLLQQGAELEMKDIHGWTALFHCTSAGHQQMVKFLLESGANANVREpVYGYTPLMEAAASGHEIIVQY 187
Cdd:PHA02874 101 ----CIEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIED-DNGCYPIHIAIKHNFFDIIKL 175

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 568996333 188 FLNHGVKVDTRDHSGATACMLARQFGHMKIVALMETHS 225
Cdd:PHA02874 176 LLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHG 213
Ank_4 pfam13637
Ankyrin repeats (many copies);
39-89 5.05e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.88  E-value: 5.05e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568996333   39 LHTAASIGQHEVVKECVQRGeLDLNKKNGGGWTALMYASYIGHDTIVHLLL 89
Cdd:pfam13637   5 LHAAAASGHLELLRLLLEKG-ADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
88-139 1.14e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.80  E-value: 1.14e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568996333   88 LLEAG-VSVNVPTPEGQTPLMLASSCGNESIAYFLLQQGAELEMKDIHGWTAL 139
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
SAM_sec23ip cd09584
SAM domain of sec23ip; SAM (sterile alpha motif) domain of Sec23ip (Sec23 interacting protein) ...
 428-477 1.21e-06

SAM domain of sec23ip; SAM (sterile alpha motif) domain of Sec23ip (Sec23 interacting protein) group is a potential protein-protein interaction domain. Sec23ip proteins (also known as p125) contain an N-terminal proline-rich region, a central region containing a SAM domain and a C-terminal region with a predicted metal-binding domain. Sec23ip interacts with Sec23p/Sec24p part of COPII-coated vesicles complex involved in protein transport from the ER to the Golgi apparatus. The proline-rich region plays an essential role in this interaction. Overexpression of Sec23ip leads to disorganization of ER/Golgi intermediate compartment.


Pssm-ID: 188983  Cd Length: 69  Bit Score: 46.34  E-value: 1.21e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 568996333 428 DLATLLEQIGCLKYLQVFEEQDIDLRIFLTLTESDLKEIGITLfGPKRKM 477
Cdd:cd09584   11 SLQSVLEALSLSEYKSTFEKEKIDMESLLMCTVDDLKEMGIPL-GPRKKI 59
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 84-209 1.85e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 51.22  E-value: 1.85e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996333  84 IVHLLLEAGVSVNVPTPEGQTPLMLASSCG--NESIAYfLLQQGAELEMKDIHGWTALFHCTSAG-HQQMVKFLLESGAN 160
Cdd:PHA02876 289 LVPKLLERGADVNAKNIKGETPLYLMAKNGydTENIRT-LIMLGADVNAADRLYITPLHQASTLDrNKDIVITLLELGAN 367

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 568996333 161 ANVREpVYGYTPLMEAAASGHEIIVQYFLNHGVKVDTRDHSGATACMLA 209
Cdd:PHA02876 368 VNARD-YCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFA 415
Ank_2 pfam12796
Ankyrin repeats (3 copies);
173-221 2.12e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 46.26  E-value: 2.12e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 568996333  173 LMEAAASGHEIIVQYFLNHGVKVDTRDHSGATACMLARQFGHMKIVALM 221
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLL 49
SAM_BOI-like_fungal cd09535
SAM domain of BOI-like fungal subfamily; SAM (sterile alpha motif) domain of BOI-like fungal ...
 426-481 2.98e-06

SAM domain of BOI-like fungal subfamily; SAM (sterile alpha motif) domain of BOI-like fungal subfamily is a potential protein-protein interaction domain. Proteins of this subfamily are apparently scaffold proteins, since most contain SH3 and PH domains, which are also protein-protein interaction domains, in addition to SAM domain. BOI-like proteins participate in cell cycle regulation. In particular BOI1 and BOI2 proteins of budding yeast S.cerevisiae are involved in bud formation, and POB1 protein of fission yeast S.pombe plays a role in cell elongation and separation. Among binding partners of BOI-like fungal subfamily members are such proteins as Bem1 and Cdc42 (they are known to be involved in cell polarization and bud formation).


Pssm-ID: 188934  Cd Length: 65  Bit Score: 45.24  E-value: 2.98e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568996333 426 PQDLATLLEQIGCLKYL-QVFEEQDIDLRIFLTLTESDLKEIGITLFGPKRKMTSAI 481
Cdd:cd09535    5 PEQVAEWLLSAGFDDSVcEKFRENEITGDILLELDLEDLKELDIGSFGKRFKLWNEI 61
Ank_4 pfam13637
Ankyrin repeats (many copies);
169-221 3.85e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.57  E-value: 3.85e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568996333  169 GYTPLMEAAASGHEIIVQYFLNHGVKVDTRDHSGATACMLARQFGHMKIVALM 221
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
Ank_4 pfam13637
Ankyrin repeats (many copies);
104-155 8.28e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.42  E-value: 8.28e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568996333  104 TPLMLASSCGNESIAYFLLQQGAELEMKDIHGWTALFHCTSAGHQQMVKFLL 155
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
SAM_caskin1,2_repeat2 cd09498
SAM domain of caskin protein repeat 2; SAM (sterile alpha motif) domain repeat 2 of caskin1,2 ...
 426-483 8.83e-06

SAM domain of caskin protein repeat 2; SAM (sterile alpha motif) domain repeat 2 of caskin1,2 proteins is a protein-protein interaction domain. Caskin has two tandem SAM domains. Caskin protein is known to interact with membrane-associated guanylate kinase CASK, and may play a role in neural development, synaptic protein targeting, and regulation of gene expression.


Pssm-ID: 188897  Cd Length: 71  Bit Score: 43.82  E-value: 8.83e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 568996333 426 PQDLATLLEQIGCLKYLQVFEEQDID-LRIFLTLTESDLKEIGITLFGPKRKMTSAIAR 483
Cdd:cd09498    7 PNDLLEWLSLLGLPQYHKVLVENGYDsIDFVTDLTWEDLQDIGITKLGHQKKLMLAIKK 65
SAM_Ste11_fungal cd09534
SAM domain of Ste11_fungal subfamily; SAM (sterile alpha motif) domain of Ste11 subfamily is a ...
 424-481 9.52e-06

SAM domain of Ste11_fungal subfamily; SAM (sterile alpha motif) domain of Ste11 subfamily is a protein-protein interaction domain. Proteins of this subfamily have SAM domain at the N-terminus and protein kinase domain at the C-terminus. They participate in regulation of mating pheromone response, invasive growth and high osmolarity growth response. MAP triple kinase Ste11 from S.cerevisia is known to interact with Ste20 kinase and Ste50 regulator. These kinases are able to form homodimers interacting through their SAM domains as well as heterodimers or heterogenous complexes when either SAM domain of monomeric or homodimeric form of Ste11 interacts with Ste50 regulator.


Pssm-ID: 188933  Cd Length: 62  Bit Score: 43.35  E-value: 9.52e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 568996333 424 SGPQDLATLLEQIGCLKYLQVFEEQDIDLRIFLTLTESDLKEIGITLFGPKRKMTSAI 481
Cdd:cd09534    1 WDEEFVEEWLNELNCGQYLDIFEKNLITGDLLLELDKEALKELGITKVGDRIRLLRAI 58
PHA02798 PHA02798
ankyrin-like protein; Provisional
 84-173 1.02e-05

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 48.68  E-value: 1.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996333  84 IVHLLLEAGVSVNVPTPEGQTPL--MLASS-CGNESIAYFLLQQGAELEMKDIHGWTALFHCTSAGHQ---QMVKFLLES 157
Cdd:PHA02798  91 IVKILIENGADINKKNSDGETPLycLLSNGyINNLEILLFMIENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEK 170

                         90
                 ....*....|....*.
gi 568996333 158 GANANVREPVYGYTPL 173
Cdd:PHA02798 171 GVDINTHNNKEKYDTL 186
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 117-204 2.94e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 47.18  E-value: 2.94e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996333 117 IAYFLLQQGAELEMKDIH-GWTALFHCTSAGHQQMVKFLLESGANANVREPVYGYtPLMEAAASGHEIIVQYFLNHGVKV 195
Cdd:PHA02878 149 ITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNS-PLHHAVKHYNKPIVHILLENGAST 227


                 ....*....
gi 568996333 196 DTRDHSGAT 204
Cdd:PHA02878 228 DARDKCGNT 236
SAM_DDHD2 cd09585
SAM domain of DDHD2; SAM (sterile alpha motif) domain of DDHD2 group is a potential ...
 429-483 3.32e-05

SAM domain of DDHD2; SAM (sterile alpha motif) domain of DDHD2 group is a potential protein-protein interaction domain. DDHD2 proteins contain at least two domains:a SAM domain and a predicted metal-binding domain. Phospholipase A1 activity was demonstrated for the mammalian DDHD2 protein. Mutation of the putative catalytic serine resulted in elimination of activity. Unlike SEC23IP, DDHD2 proteins do not have an N-terminal proline-rich region and correspondingly they are not able to interact with Sec23p/Sec24p complex. Overexpression of DDHD2 is the cause of dispersion of ER/Golgi intermediate compartment and dispersion of tethering proteins located in the Golgi region, leading to aggregation in the endoplasmic reticulum.


Pssm-ID: 188984  Cd Length: 69  Bit Score: 42.43  E-value: 3.32e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568996333 429 LATLLEQIGCLKYLQVFEEQDIDLRIFLTLTESDLKEIGITLfGPKRKMTSAIAR 483
Cdd:cd09585   12 LEETLKKLGLSEYCDVFEKEKIDLEALALCQERDLKDLGIPL-GPRKKILNYIRR 65
PHA03095 PHA03095
ankyrin-like protein; Provisional
 49-128 3.50e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 46.94  E-value: 3.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996333  49 EVVKECVQRGeLDLNKKNGGGWTALMYASYIG--HDTIVHLLLEAGVSVNVPTPEGQTPLMLASSCGNESIAYFLLQQGA 126
Cdd:PHA03095 203 RIVRELIRAG-CDPAATDMLGNTPLHSMATGSscKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGA 281


                 ..
gi 568996333 127 EL 128
Cdd:PHA03095 282 DI 283
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 168-197 6.49e-05

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 40.32  E-value: 6.49e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 568996333  168 YGYTPLMEAAASGHEIIVQYFLNHGVKVDT 197
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
SAM_DGK-delta-eta cd09507
SAM domain of diacylglycerol kinase delta and eta subunits; SAM (sterile alpha motif) domain ...
 422-482 8.13e-05

SAM domain of diacylglycerol kinase delta and eta subunits; SAM (sterile alpha motif) domain of DGK-eta-delta subfamily proteins is a protein-protein interaction domain. Proteins of this subfamily are multidomain diacylglycerol kinases with a SAM domain located at the C-terminus. DGK proteins participate in signal transduction. They regulate the level of second messengers such as diacylglycerol and phosphatidic acid. The SAM domain of DGK proteins can form high molecular weight homooligomers through head-to-tail interactions as well as heterooligomers between the SAM domains of DGK delta and eta proteins. The oligomerization plays a role in the regulation of DGK intracellular localization.


Pssm-ID: 188906  Cd Length: 65  Bit Score: 40.86  E-value: 8.13e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568996333 422 PYSGPQDLATLLEQIGCLKYLQVFEEQDIDLRIFLTLTESDLKEIGITLFGPKRKMTSAIA 482
Cdd:cd09507    3 TNWTTEEVGAWLESLQLGEYRDIFARNDIRGSELLHLERRDLKDLGITKVGHVKRILQAIK 63
SAM_ASZ1 cd09521
SAM domain of ASZ1 subfamily; SAM (sterile alpha motif) domain of ASZ1 (Ankyrin, SAM, leucine ...
 423-485 1.14e-04

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: 40.73  E-value: 1.14e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568996333 423 YSGPQDLATLLEQIGCLKYLQVFEEQDIDLRIFLTLTESDLKEIGITLFGPKRKMTSAIARWH 485
Cdd:cd09521    2 YSKLDDLELFLHGLELGHLTPLFKEHDVTFSQLLKMTEEDLEKIGITQPGDQKKILDAIKEVH 64
SAM_TAL cd09523
SAM domain of TAL subfamily; SAM (sterile alpha motif) domain of TAL (Tsg101-associated ligase) ...
 428-485 1.34e-04

SAM domain of TAL subfamily; SAM (sterile alpha motif) domain of TAL (Tsg101-associated ligase) proteins, also known as LRSAM1 (Leucine-rich repeat and sterile alpha motif-containing) proteins, is a putative protein-protein interaction domain. Proteins of this subfamily participate in the regulation of retrovirus budding and receptor endocytosis. They show E3 ubiquitin ligase activity. Human TAL protein interacts with Tsg101 and TAL's C-terminal ring finger domain is essential for the multiple monoubiquitylation of Tsg101.


Pssm-ID: 188922  Cd Length: 65  Bit Score: 40.35  E-value: 1.34e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 568996333 428 DLATLLEQIGCLKYLQVFEEQDIDLRIFLTLTESDLKEIGITLFGPKRKMTSAIARWH 485
Cdd:cd09523    7 QLVNLLNELSAEHYLPVFARHRITMETLSTMTDEDLKKIGIHEIGLRKEILRAAQELL 64
Ank_5 pfam13857
Ankyrin repeats (many copies);
154-205 1.35e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.02  E-value: 1.35e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568996333  154 LLESGANANVREPVYGYTPLMEAAASGHEIIVQYFLNHGVKVDTRDHSGATA 205
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTA 52
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 168-196 1.41e-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: 39.49  E-value: 1.41e-04
                           10        20
                   ....*....|....*....|....*....
gi 568996333   168 YGYTPLMEAAASGHEIIVQYFLNHGVKVD 196
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 168-200 1.41e-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: 39.58  E-value: 1.41e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 568996333  168 YGYTPLMEAAAS-GHEIIVQYFLNHGVKVDTRDH 200
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 134-164 1.89e-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: 39.19  E-value: 1.89e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 568996333  134 HGWTALFH-CTSAGHQQMVKFLLESGANANVR 164
Cdd:pfam00023   1 DGNTPLHLaAGRRGNLEIVKLLLSKGADVNAR 32
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 69-99 2.13e-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: 38.81  E-value: 2.13e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 568996333   69 GWTALMYASYI-GHDTIVHLLLEAGVSVNVPT 99
Cdd:pfam00023   2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 139-251 3.34e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 43.73  E-value: 3.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996333 139 LFHCTSAGHQQMVKFLLESGANANVREpVYGYTPLMEAAASGHEIIVQYFLNHGVKVDTRDHSGATACMLARQFGHMKIV 218
Cdd:PTZ00322  86 LCQLAASGDAVGARILLTGGADPNCRD-YDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVV 164

                         90       100       110
                 ....*....|....*....|....*....|....
gi 568996333 219 ALMETHSPVLPKSLYRS-PEKYEDLSSSDESWPV 251
Cdd:PTZ00322 165 QLLSRHSQCHFELGANAkPDSFTGKPPSLEDSPI 198
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 69-97 3.50e-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: 3.50e-04
                           10        20
                   ....*....|....*....|....*....
gi 568996333    69 GWTALMYASYIGHDTIVHLLLEAGVSVNV 97
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 61-132 3.58e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 43.50  E-value: 3.58e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568996333  61 DLNKKNGGGWTALMYASYIGHDTIVHLLLEAGVSVNVPTPEGQTPLMLASSCGNESIAYFLLQQGAELEMKD 132
Cdd:PHA03100 184 PINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTII 255
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 69-190 6.06e-04

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 43.08  E-value: 6.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996333  69 GWTALMYASYIGHDTIVHLLLEAGVSVNVPTPEG--------------QTPLMLASSCGNESIAYFLLQQGAELEMKDIH 134
Cdd:cd22192   89 GETALHIAVVNQNLNLVRELIARGADVVSPRATGtffrpgpknliyygEHPLSFAACVGNEEIVRLLIEHGADIRAQDSL 168

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568996333 135 GWTALFHCTSAGHQ----QMVKFLLESGANANvREPVY------GYTPLMEAAASGHEIIVQYFLN 190
Cdd:cd22192  169 GNTVLHILVLQPNKtfacQMYDLILSYDKEDD-LQPLDlvpnnqGLTPFKLAAKEGNIVMFQHLVQ 233
SAM_tankyrase1,2 cd09524
SAM domain of tankyrase1,2 subfamily; SAM (sterile alpha motif) domain of Tankyrase1,2 ...
 428-483 1.27e-03

SAM domain of tankyrase1,2 subfamily; SAM (sterile alpha motif) domain of Tankyrase1,2 subfamily is a protein-protein interaction domain. In addition to the SAM domain, proteins of this group have ankyrin repeats and a ADP- ribosyltransferase (poly-(ADP-ribose) synthase) domain. Tankyrases can polymerize through their SAM domains forming homoligomers and these complexes are disrupted by autoribosylation. Tankyrases apparently act as master scaffolding proteins and thus may interact simultaneously with multiple proteins, in particular with TRF1, NuMA, IRAP and Grb14 (ankyrin repeats are involved in these interactions). Tankyrases participate in a variety of cell signaling pathways as effector molecules. Their functions are different depending on the intracellular location: at telomeres they play a role in the regulation of telomere length via control of telomerase access to telomeres, at centrosomes they promote spindle assembly/disassembly, in Golgi vesicles they participate in the regulation of vesicle trafficking and Golgi dynamics. Tankyrase 1 may be of interest as new potential target for telomerase-directed cancer therapy.


Pssm-ID: 188923  Cd Length: 66  Bit Score: 37.69  E-value: 1.27e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 568996333 428 DLATLLEQIGCLKYLQVFEEQDIDLRIFLTLTESDLKEIGITLFGPKRKMTSAIAR 483
Cdd:cd09524    7 SISQFLSSLGLEHLREIFEREQITLDVLAEMGHEELKEIGINAYGHRHKLIKGVER 62
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 101-132 1.55e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 36.50  E-value: 1.55e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 568996333  101 EGQTPLMLAS-SCGNESIAYFLLQQGAELEMKD 132
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 69-97 1.88e-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: 36.08  E-value: 1.88e-03
                          10        20
                  ....*....|....*....|....*....
gi 568996333   69 GWTALMYASYIGHDTIVHLLLEAGVSVNV 97
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 134-163 2.53e-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: 35.64  E-value: 2.53e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 568996333   134 HGWTALFHCTSAGHQQMVKFLLESGANANV 163
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 34-162 2.67e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 40.82  E-value: 2.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996333  34 DVPLDLHTAASI-GQHE-------VVKECVQRGELDLNKKNGGGWTALMYASYIGHDT--IVHLLLEAGVSVNVPTPEGQ 103
Cdd:PHA02876 100 DIILDIKYASIIlNKHKldeacihILKEAISGNDIHYDKINESIEYMKLIKERIQQDEllIAEMLLEGGADVNAKDIYCI 179

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 568996333 104 TPLMLASSCGNESIAYFLLQQGAELEMKDIHGWTALFHCTSAGHQQMVKFLLESGANAN 162
Cdd:PHA02876 180 TPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNIN 238
PHA02791 PHA02791
ankyrin-like protein; Provisional
 132-220 2.96e-03

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 40.03  E-value: 2.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996333 132 DIHGWTALFHCTSAGHQQMVKFLLESGANANVREPVYgytPLMEAAASGHEIIVQYFLNHGVKVDTRDHSGATACMLARQ 211
Cdd:PHA02791  27 DVHGHSALYYAIADNNVRLVCTLLNAGALKNLLENEF---PLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVD 103


                 ....*....
gi 568996333 212 FGHMKIVAL 220
Cdd:PHA02791 104 SGNMQTVKL 112
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 25-177 2.99e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 40.65  E-value: 2.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996333  25 GAQGSPEELDVPLDLHTAASIgQHEVVKECVQRGELDL--NKKNGGGWTA-----------------LMYASYIGHDTIV 85
Cdd:PTZ00322  20 GTEGSRKRRAKPISFERMAAI-QEEIARIDTHLEALEAteNKDATPDHNLtteevidpvvahmltveLCQLAASGDAVGA 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996333  86 HLLLEAGVSVNVPTPEGQTPLMLASSCGNESIAYFLLQQGAELEMKDIHGWTALFHCTSAGHQQMVKFLL-------ESG 158
Cdd:PTZ00322  99 RILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSrhsqchfELG 178

                        170       180
                 ....*....|....*....|....
gi 568996333 159 ANA-----NVREPVYGYTPLMEAA 177
Cdd:PTZ00322 179 ANAkpdsfTGKPPSLEDSPISSHH 202
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 39-139 3.49e-03

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 40.83  E-value: 3.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996333   39 LHtAASIGQHEVVKECVQRgELDLNKKNGGGW--------------TALMYASYIGHDTIVHLLLEAGVSVN-------- 96
Cdd:TIGR00870  86 LH-AISLEYVDAVEAILLH-LLAAFRKSGPLElandqytseftpgiTALHLAAHRQNYEIVKLLLERGASVParacgdff 163

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 568996333   97 VPTPE------GQTPLMLASSCGNESIAYFLLQQGAELEMKDIHGWTAL 139
Cdd:TIGR00870 164 VKSQGvdsfyhGESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLL 212
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 42-173 3.74e-03

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: 40.38  E-value: 3.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996333  42 AASIGQHEVVKECVQRGELDLNKKNGGGWTALMYASYIGHDTIVHLLLEAG-VSVNVPTP----EGQTPLMLASSCGNES 116
Cdd:cd22192   24 AAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAApELVNEPMTsdlyQGETALHIAVVNQNLN 103

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568996333 117 IAYFLLQQGAELEMKDIHGW------TALFH----------CTsaGHQQMVKFLLESGANANVREPvYGYTPL 173
Cdd:cd22192  104 LVRELIARGADVVSPRATGTffrpgpKNLIYygehplsfaaCV--GNEEIVRLLIEHGADIRAQDS-LGNTVL 173
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 84-199 6.04e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 39.72  E-value: 6.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996333  84 IVHLLLEAGVSVNVPTPEGQTPLM---LASSCGNESIAYFLLQQGAEL-EMKDIHGWTaLFHCTSAG---HQQMVKFLLE 156
Cdd:PHA02989  90 IVKLLLKFGADINLKTFNGVSPIVcfiYNSNINNCDMLRFLLSKGINVnDVKNSRGYN-LLHMYLESfsvKKDVIKILLS 168

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 568996333 157 SGANANVREPVYGYTPL---MEAAASGHEI-IVQYFLNHGVKVDTRD 199
Cdd:PHA02989 169 FGVNLFEKTSLYGLTPMniyLRNDIDVISIkVIKYLIKKGVNIETNN 215
SAM_HARP cd09587
SAM domain of HARP subfamily; SAM (sterile alpha motif) domain of HARP (Harmonin-interacting ...
 429-491 6.31e-03

SAM domain of HARP subfamily; SAM (sterile alpha motif) domain of HARP (Harmonin-interacting Ankyrin Repeat-containing) proteins, also known as ANKS4B, is a protein-protein interaction domain. Proteins of this subfamily have an N-terminal ankyrin repeat region and C-terminal SAM. In mouse epithelial tissues, HARP protein interacts with the PDZ domain of harmonin. This scaffolding complex facilitates signal transduction in epithelia. HARP was found co-expressed with harmonin in a number of epithelial cells including pancreatic ductal epithelium, embryonic epithelia of the lung, kidney, salivary glands, and cochlea.


Pssm-ID: 188986  Cd Length: 67  Bit Score: 35.96  E-value: 6.31e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568996333 429 LATLLEQIGCLKYLQVFEEQDIDLRIFLTLTESDLKEIGITLfGPKRKMTSAIARWHSSARPP 491
Cdd:cd09587    5 LEVFLSSQHLEEFLPIFMREQIDLEALMLCSDEDLQNIQMQL-GPRKKILSAVARRKQVLQQP 66
PHA02946 PHA02946
ankyin-like protein; Provisional
 82-202 6.57e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 39.65  E-value: 6.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996333  82 DTIVHLLLEAGVSVNVPTPEGQTPLMLASSCGNESIAYFLLQQGAELEMKDIHGWTALFHCTSAGHQ--QMVKFLLESGA 159
Cdd:PHA02946  52 ERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEviERINLLVQYGA 131

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 568996333 160 NANVREPVYGYTPLMeAAASGHEIIVQYFLNHGVKVDTRDHSG 202
Cdd:PHA02946 132 KINNSVDEEGCGPLL-ACTDPSERVFKKIMSIGFEARIVDKFG 173
SAM_Polycomb cd09509
SAM domain of Polycomb group; SAM (sterile alpha motif) domain of Polycomb group is a ...
 437-483 7.72e-03

SAM domain of Polycomb group; SAM (sterile alpha motif) domain of Polycomb group is a protein-protein interaction domain. The Polycomb group includes transcriptional repressors which are involved in the regulation of some key regulatory genes during development in many organisms. They are best known for silencing Hox (Homeobox) genes. Polycomb proteins work together in large multimeric and chromatin-associated complexes. They organize chromatin of the target genes and maintain repressed states during many cell divisions. Polycomb proteins are classified based on their common function, but not on conserved domains and/or motifs; however many Polycomb proteins (members of PRC1 class complex) contain SAM domains which are more similar to each other inside of the Polycomb group than to SAM domains outside of it. Most information about structure and function of Polycomb SAM domains comes from studies of Ph (Polyhomeotic) and Scm (Sex comb on midleg) proteins. Polycomb SAM domains usually can be found at the C-terminus of the proteins. Some members of this group contain, in addition to the SAM domain, MTB repeats, Zn finger, and/or DUF3588 domains. Polycomb SAM domains can form homo- and/or heterooligomers through ML and EH surfaces. SAM/SAM oligomers apparently play a role in transcriptional repression through polymerization along the chromosome. Polycomb proteins are known to be highly expressed in some cells years before their cancer pathology; thus they are attractive markers for early cancer therapy.


Pssm-ID: 188908  Cd Length: 64  Bit Score: 35.53  E-value: 7.72e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 568996333 437 GCLKYLQVFEEQDIDLRIFLTLTESDL-KEIGITLfGPKRKMTSAIAR 483
Cdd:cd09509   18 GCAEYAEVFREQEIDGQALLLLTEDDLlKGMGLKL-GPALKIYNHIVK 64
SAM_SARM1-like_repeat1 cd09501
SAM domain ot SARM1-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 428-483 7.78e-03

SAM domain ot SARM1-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of SARM1-like adaptor proteins is a protein-protein interaction domain. SARM1-like proteins contain two tandem SAM domains. SARM1-like proteins are involved in TLR (Toll-like receptor) signaling. They are responsible for targeted localization of the whole protein to post-synaptic regions of axons. In humans SARM1 expression is detected in kidney and liver.


Pssm-ID: 188900 [Multi-domain]  Cd Length: 69  Bit Score: 35.74  E-value: 7.78e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568996333 428 DLATLLEQIGCLKYLQVFEEQDIDLRIFLTLTESDLKE-IGitlfgpkrkMTSAIAR 483
Cdd:cd09501    8 DVQTWLKQIGFEDYAEKFSESQVDGDLLLQLTEDELKQdLG---------MSSGLLR 55
PHA02791 PHA02791
ankyrin-like protein; Provisional
 61-190 8.05e-03

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 38.87  E-value: 8.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996333  61 DLNKKNGGGWTALMYASYIGHDTIVHLLLEAGVSVNVPtpEGQTPLMLASSCGNESIAYFLLQQGAELEMKDIHGWTALF 140
Cdd:PHA02791  22 DAFKADVHGHSALYYAIADNNVRLVCTLLNAGALKNLL--ENEFPLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALY 99

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568996333 141 HCTSAGHQQMVKFLLESganaNVREPVYG----YTPLMEAAASGHEIIVQYFLN 190
Cdd:PHA02791 100 YAVDSGNMQTVKLFVKK----NWRLMFYGktgwKTSFYHAVMLNDVSIVSYFLS 149
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 101-130 8.47e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 34.49  E-value: 8.47e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 568996333   101 EGQTPLMLASSCGNESIAYFLLQQGAELEM 130
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 101-130 9.18e-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: 9.18e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 568996333  101 EGQTPLMLASSCGNESIAYFLLQQGAELEM 130
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
 
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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