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Conserved domains on  [gi|1907119810|ref|XP_036016036|]
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ankyrin repeat and SAM domain-containing protein 3 isoform X8 [Mus musculus]

Protein Classification

ANKYR and SAM_ANKS3 domain-containing protein( domain architecture ID 12789526)

ANKYR and SAM_ANKS3 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-151 1.78e-41

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 151.65  E-value: 1.78e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907119810   1 MYASYIGHDTIVHLLLEAGVSVNVPTPEGQTPLMLASSCGNESIAYFLLQQGAELEMKDIHGWTALFHCTSAGHQQMVKF 80
Cdd:COG0666    92 HAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKL 171

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907119810  81 LLESGANANVREPvYGYTPLMEAAASGHEIIVQYFLNHGVKVDTRDHSGATACMLARQFGHMKIVALMETH 151
Cdd:COG0666   172 LLEAGADVNARDN-DGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241
SAM_ANKS3 cd09519
SAM domain of ANKS3 subfamily; SAM (sterile alpha motif) domain of ANKS3 subfamily is a ...
 350-413 1.10e-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: 133.39  E-value: 1.10e-37
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907119810 350 YSGPQDLATLLEQIGCLKYLQVFEEQDIDLRIFLTLTESDLKEIGITLFGPKRKMTSAIARWHS 413
Cdd:cd09519     1 YTGPKDLSELLEQIGCSKYLPIFEEQDIDLRIFLTLTESDLKEIGITLFGPKRKMTSAIARWHS 64
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-151 1.78e-41

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 151.65  E-value: 1.78e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907119810   1 MYASYIGHDTIVHLLLEAGVSVNVPTPEGQTPLMLASSCGNESIAYFLLQQGAELEMKDIHGWTALFHCTSAGHQQMVKF 80
Cdd:COG0666    92 HAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKL 171

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907119810  81 LLESGANANVREPvYGYTPLMEAAASGHEIIVQYFLNHGVKVDTRDHSGATACMLARQFGHMKIVALMETH 151
Cdd:COG0666   172 LLEAGADVNARDN-DGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241
SAM_ANKS3 cd09519
SAM domain of ANKS3 subfamily; SAM (sterile alpha motif) domain of ANKS3 subfamily is a ...
 350-413 1.10e-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: 133.39  E-value: 1.10e-37
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907119810 350 YSGPQDLATLLEQIGCLKYLQVFEEQDIDLRIFLTLTESDLKEIGITLFGPKRKMTSAIARWHS 413
Cdd:cd09519     1 YTGPKDLSELLEQIGCSKYLPIFEEQDIDLRIFLTLTESDLKEIGITLFGPKRKMTSAIARWHS 64
Ank_2 pfam12796
Ankyrin repeats (3 copies);
33-126 7.59e-23

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.87  E-value: 7.59e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907119810  33 LMLASSCGNESIAYFLLQQGAELEMKDIHGWTALFHCTSAGHQQMVKFLLEsgaNANVREPVYGYTPLMEAAASGHEIIV 112
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE---HADVNLKDNGRTALHYAARSGHLEIV 77

                          90
                  ....*....|....
gi 1907119810 113 QYFLNHGVKVDTRD 126
Cdd:pfam12796  78 KLLLEKGADINVKD 91
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 15-173 1.69e-15

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 79.91  E-value: 1.69e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907119810  15 LLEAGVSVNVPTPEGQTPLMLASSCGNESIAYFLLQQGAELEMKDIHGWTALFHCTSAGHQQMVKFLLESganANVREPV 94
Cdd:PLN03192  544 LLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHF---ASISDPH 620

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907119810  95 YGYTPLMEAAASGHEIIVQYFLNHGVKVDTRDHSGATACMLARQFGHMKIVALMETHSPVLPKSlyrspEKYEDLSSSD 173
Cdd:PLN03192  621 AAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKA-----NTDDDFSPTE 694
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 350-411 2.53e-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: 59.21  E-value: 2.53e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907119810 350 YSGPQDLATLLEQIGCLKYLQVFEEQDIDLRIFLTLTESDLKEIGITLFGPKRKMTSAIARW 411
Cdd:pfam00536   2 GWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLKLGVTLLGHRKKILYAIQRL 63
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 349-408 2.02e-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: 56.92  E-value: 2.02e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907119810  349 PYSGPQDLATLLEQIGCLKYLQVFEEQDIDLRIFLTLT-ESDLKEIGITLFGPKRKMTSAI 408
Cdd:smart00454   2 SQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTsEEDLKELGITKLGHRKKILKAI 62
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 95-123 1.20e-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: 1.20e-04
                           10        20
                   ....*....|....*....|....*....
gi 1907119810   95 YGYTPLMEAAASGHEIIVQYFLNHGVKVD 123
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 10-117 2.60e-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: 40.77  E-value: 2.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907119810  10 TIVHLLLEAGVSVNVPTPEG--------------QTPLMLASSCGNESIAYFLLQQGAELEMKDIHGWTALFHCTSAGHQ 75
Cdd:cd22192   103 NLVRELIARGADVVSPRATGtffrpgpknliyygEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNK 182

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907119810  76 ----QMVKFLLESGANANvREPVY------GYTPLMEAAASGHEIIVQYFLN 117
Cdd:cd22192   183 tfacQMYDLILSYDKEDD-LQPLDlvpnnqGLTPFKLAAKEGNIVMFQHLVQ 233
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-151 1.78e-41

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 151.65  E-value: 1.78e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907119810   1 MYASYIGHDTIVHLLLEAGVSVNVPTPEGQTPLMLASSCGNESIAYFLLQQGAELEMKDIHGWTALFHCTSAGHQQMVKF 80
Cdd:COG0666    92 HAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKL 171

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907119810  81 LLESGANANVREPvYGYTPLMEAAASGHEIIVQYFLNHGVKVDTRDHSGATACMLARQFGHMKIVALMETH 151
Cdd:COG0666   172 LLEAGADVNARDN-DGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241
SAM_ANKS3 cd09519
SAM domain of ANKS3 subfamily; SAM (sterile alpha motif) domain of ANKS3 subfamily is a ...
 350-413 1.10e-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: 133.39  E-value: 1.10e-37
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907119810 350 YSGPQDLATLLEQIGCLKYLQVFEEQDIDLRIFLTLTESDLKEIGITLFGPKRKMTSAIARWHS 413
Cdd:cd09519     1 YTGPKDLSELLEQIGCSKYLPIFEEQDIDLRIFLTLTESDLKEIGITLFGPKRKMTSAIARWHS 64
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-148 2.31e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 137.39  E-value: 2.31e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907119810   1 MYASYIGHDTIVHLLLEAGVSVNVPTPEGQTPLMLASSCGNESIAYFLLQQGAELEMKDIHGWTALFHCTSAGHQQMVKF 80
Cdd:COG0666   125 HLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKL 204

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907119810  81 LLESGANANVREPvYGYTPLMEAAASGHEIIVQYFLNHGVKVDTRDHSGATACMLARQFGHMKIVALM 148
Cdd:COG0666   205 LLEAGADVNAKDN-DGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLL 271
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-147 2.76e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 137.39  E-value: 2.76e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907119810   1 MYASYIGHDTIVHLLLEAGVSVNVPTPEGQTPLMLASSCGNESIAYFLLQQGAELEMKDIHGWTALFHCTSAGHQQMVKF 80
Cdd:COG0666    59 LAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKL 138

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907119810  81 LLESGANANVREPvYGYTPLMEAAASGHEIIVQYFLNHGVKVDTRDHSGATACMLARQFGHMKIVAL 147
Cdd:COG0666   139 LLEAGADVNAQDN-DGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKL 204
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-148 1.27e-24

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 104.27  E-value: 1.27e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907119810   1 MYASYIGHDTIVHLLLEAGVSVNVPTPEGQTPLMLASSCGNESIAYFLLQQGAELEMKDIHGWTALFHCTSAGHQQMVKF 80
Cdd:COG0666    26 LAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKL 105

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907119810  81 LLESGANANVREPvYGYTPLMEAAASGHEIIVQYFLNHGVKVDTRDHSGATACMLARQFGHMKIVALM 148
Cdd:COG0666   106 LLEAGADVNARDK-DGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLL 172
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-132 5.95e-24

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 102.34  E-value: 5.95e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907119810   1 MYASYIGHDTIVHLLLEAGVSVNVPTPEGQTPLMLASSCGNESIAYFLLQQGAELEMKDIHGWTALFHCTSAGHQQMVKF 80
Cdd:COG0666   158 HLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKL 237

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907119810  81 LLESGANANVREPvYGYTPLMEAAASGHEIIVQYFLNHGVKVDTRDHSGATA 132
Cdd:COG0666   238 LLEAGADLNAKDK-DGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
Ank_2 pfam12796
Ankyrin repeats (3 copies);
33-126 7.59e-23

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.87  E-value: 7.59e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907119810  33 LMLASSCGNESIAYFLLQQGAELEMKDIHGWTALFHCTSAGHQQMVKFLLEsgaNANVREPVYGYTPLMEAAASGHEIIV 112
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE---HADVNLKDNGRTALHYAARSGHLEIV 77

                          90
                  ....*....|....
gi 1907119810 113 QYFLNHGVKVDTRD 126
Cdd:pfam12796  78 KLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1-91 8.14e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 89.79  E-value: 8.14e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907119810   1 MYASYIGHDTIVHLLLEAGVSVNVPTPEGQTPLMLASSCGNESIAYFLLQQgAELEMKDiHGWTALFHCTSAGHQQMVKF 80
Cdd:pfam12796   2 HLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVKL 79

                          90
                  ....*....|.
gi 1907119810  81 LLESGANANVR 91
Cdd:pfam12796  80 LLEKGADINVK 90
SAM_BICC1 cd09520
SAM domain of BICC1 (bicaudal) subfamily; SAM (sterile alpha motif) domain of BICC1 (bicaudal) ...
 350-409 2.20e-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: 2.20e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907119810 350 YSGPQDLATLLEQIGCLKYLQVFEEQDIDLRIFLTLTESDLKEIGITLFGPKRKMTSAIA 409
Cdd:cd09520     1 SAKYSDLPELLAKLGLEKYIDLFAQQEIDLQTFLTLTDQDLKELGITAFGARRKMLLAIS 60
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 15-173 1.69e-15

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 79.91  E-value: 1.69e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907119810  15 LLEAGVSVNVPTPEGQTPLMLASSCGNESIAYFLLQQGAELEMKDIHGWTALFHCTSAGHQQMVKFLLESganANVREPV 94
Cdd:PLN03192  544 LLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHF---ASISDPH 620

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907119810  95 YGYTPLMEAAASGHEIIVQYFLNHGVKVDTRDHSGATACMLARQFGHMKIVALMETHSPVLPKSlyrspEKYEDLSSSD 173
Cdd:PLN03192  621 AAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKA-----NTDDDFSPTE 694
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 355-410 4.43e-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: 66.88  E-value: 4.43e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907119810 355 DLATLLEQIGCLKYLQVFEEQDIDLRIFLTLTESDLKEIGITLFGPKRKMTSAIAR 410
Cdd:cd09487     1 DVAEWLESLGLEQYADLFRKNEIDGDALLLLTDEDLKELGITSPGHRKKILRAIQR 56
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
11-147 8.99e-13

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 69.21  E-value: 8.99e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907119810  11 IVHLLLEAGVSVNVPTPEGQTPLMLASSCGNESIAYFLLQQGAELEMKDIHGWTALFHCTSAGHQQMVKFLLESGANANV 90
Cdd:COG0666     3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907119810  91 REPvYGYTPLMEAAASGHEIIVQYFLNHGVKVDTRDHSGATACMLARQFGHMKIVAL 147
Cdd:COG0666    83 KDD-GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKL 138
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 6-124 4.36e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 68.15  E-value: 4.36e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907119810   6 IGHDTIVHLLLEAGVSVNVPTPEGQTPLMLASSCGNE--SIAYFLLQQGA------ELEM----------KDIHGWTALF 67
Cdd:PHA03100  118 SNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVdinaknRVNYllsygvpiniKDVYGFTPLH 197

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907119810  68 HCTSAGHQQMVKFLLESGANANVREpVYGYTPLMEAAASGHEIIVQYFLNHGVKVDT 124
Cdd:PHA03100  198 YAVYNNNPEFVKYLLDLGANPNLVN-KYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 350-411 2.53e-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: 59.21  E-value: 2.53e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907119810 350 YSGPQDLATLLEQIGCLKYLQVFEEQDIDLRIFLTLTESDLKEIGITLFGPKRKMTSAIARW 411
Cdd:pfam00536   2 GWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLKLGVTLLGHRKKILYAIQRL 63
PHA03095 PHA03095
ankyrin-like protein; Provisional
 1-132 4.96e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 65.05  E-value: 4.96e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907119810   1 MYASYIGHDT--IVHLLLEAGVSVNVPTPEGQTPLMLASSCGN-ESIAYFLLQQGAELEMKDIHGWTAL-FHCTS-AGHQ 75
Cdd:PHA03095   53 LYLHYSSEKVkdIVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKAGADVNAKDKVGRTPLhVYLSGfNINP 132

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907119810  76 QMVKFLLESGANANVREpVYGYTPLmEAAASGHEI---IVQYFLNHGVKVDTRDHSGATA 132
Cdd:PHA03095  133 KVIRLLLRKGADVNALD-LYGMTPL-AVLLKSRNAnveLLRLLIDAGADVYAVDDRFRSL 190
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 11-131 5.34e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 64.69  E-value: 5.34e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907119810  11 IVHLLLEAGVSVNVPTPEGQTPLMLASSC--GNESIAYFLLQQGAELEMKDIHGWTALFHCTSAGHQ--QMVKFLLESGA 86
Cdd:PHA03100   88 IVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGV 167

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907119810  87 NANVREPV---------------YGYTPLMEAAASGHEIIVQYFLNHGVKVDTRDHSGAT 131
Cdd:PHA03100  168 DINAKNRVnyllsygvpinikdvYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDT 227
SAM_ANKS6 cd09518
SAM domain of ANKS6 (or SamCystin) subfamily; SAM (sterile alpha motif) domain of ANKS6 (or ...
 355-413 1.61e-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: 1.61e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907119810 355 DLATLLEQIGCLKYLQVFEEQDIDLRIFLTLTESDLKEIGITLFGPKRKMTSAIARWHS 413
Cdd:cd09518     7 ELSGILRKLSLEKYQPIFEEQEVDMEAFLTLTDGDLKELGIKTDGPRQQILAAISELNA 65
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 349-408 2.02e-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: 56.92  E-value: 2.02e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907119810  349 PYSGPQDLATLLEQIGCLKYLQVFEEQDIDLRIFLTLT-ESDLKEIGITLFGPKRKMTSAI 408
Cdd:smart00454   2 SQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTsEEDLKELGITKLGHRKKILKAI 62
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 11-145 1.08e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 60.83  E-value: 1.08e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907119810  11 IVHLLLEAGVSVNVPTPEGQTPLMLASSCG-----NESIAYFLLQQGAELEMKDIHGWTALFHC--TSAGHQQMVKFLLE 83
Cdd:PHA03100   50 VVKILLDNGADINSSTKNNSTPLHYLSNIKynltdVKEIVKLLLEYGANVNAPDNNGITPLLYAisKKSNSYSIVEYLLD 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907119810  84 SGANANVREPvYGYTPLMEAAASGH---EII---------------VQYFLNHGVKVDTRDHSGATACMLARQFGHMKIV 145
Cdd:PHA03100  130 NGANVNIKNS-DGENLLHLYLESNKidlKILkllidkgvdinaknrVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFV 208
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 11-125 1.09e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 61.05  E-value: 1.09e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907119810  11 IVHLLLEAGVSVNVPTPE-GQTPLMLASSCGNESIAYFLLQQGAELEMKDIHGWTALFHCTSAGHQQMVKFLLESGANAN 89
Cdd:PHA02878  149 ITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTD 228

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1907119810  90 VREpVYGYTPLMEAAASGHEI-IVQYFLNHGVKVDTR 125
Cdd:PHA02878  229 ARD-KCGNTPLHISVGYCKDYdILKLLLEHGVDVNAK 264
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 11-131 1.13e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 60.75  E-value: 1.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907119810  11 IVHLLLEAGVSVNVPTPEGQTPLMLASSCGNESIAYFLLQQGAELEMKDIHGWTALFHCTSAGHQQMVKFLLESGANANV 90
Cdd:PHA02874  106 MIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANV 185

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1907119810  91 REpVYGYTPLMEAAASGHEIIVQYFLNHGVKVDTRDHSGAT 131
Cdd:PHA02874  186 KD-NNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFT 225
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
349-408 2.54e-09

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 53.43  E-value: 2.54e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907119810 349 PYSGPQDLATLLEQIGCLKYLQVFEEQDID-LRIFLTLTESDLKEIGITLFGPKRKMTSAI 408
Cdd:pfam07647   2 ESWSLESVADWLRSIGLEQYTDNFRDQGITgAELLLRLTLEDLKRLGITSVGHRRKILKKI 62
SAM_sec23ip-like cd09516
SAM domain of sec23ip-like subfamily; SAM (sterile alpha motif) domain of Sec23ip-like (Sec23 ...
 353-404 3.23e-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: 53.57  E-value: 3.23e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907119810 353 PQDLATLLEQIGCLKYLQVFEEQDIDLRIFLTLTESDLKEIGITLfGPKRKM 404
Cdd:cd09516     9 PLTLEEDLEKLGLSEYFDTFEKEKIDMESLLLCSESDLKEMGIPM-GPRKKL 59
Ank_4 pfam13637
Ankyrin repeats (many copies);
62-116 4.81e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.28  E-value: 4.81e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1907119810  62 GWTALFHCTSAGHQQMVKFLLESGANANVRePVYGYTPLMEAAASGHEIIVQYFL 116
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAV-DGNGETALHFAASNGNVEVLKLLL 54
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1-59 3.42e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 51.27  E-value: 3.42e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907119810   1 MYASYIGHDTIVHLLLEaGVSVNVpTPEGQTPLMLASSCGNESIAYFLLQQGAELEMKD 59
Cdd:pfam12796  35 HLAAKNGHLEIVKLLLE-HADVNL-KDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
SAM_USH1G_HARP cd09517
SAM domain of USH1G_HARP family; SAM (sterile alpha motif) domain of USH1G/HARP (Usher ...
 356-410 9.98e-08

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: 9.98e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1907119810 356 LATLLEQIGCLKYLQVFEEQDIDLRIFLTLTESDLKEIGITLfGPKRKMTSAIAR 410
Cdd:cd09517     5 LERFLTSNHLEEYLPVFEREKIDLEALMLLTDEDLQSLKLPL-GPRRKLLNAIAK 58
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 12-148 2.77e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 53.07  E-value: 2.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907119810  12 VHLLLEAGVSVN-VPTPEGQTPLMLASSCGNESIAYFLLQQGAELEMKDIHGWTALFHCTSAGHQQMVKFLLESGANANV 90
Cdd:PHA02875   84 VEELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDI 163

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907119810  91 rEPVYGYTPLMEAAASGHEIIVQYFLNHGVKVDTRDHSGATACM-LARQFGHMKIVALM 148
Cdd:PHA02875  164 -EDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALcYAIENNKIDIVRLF 221
Ank_5 pfam13857
Ankyrin repeats (many copies);
15-66 6.33e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.57  E-value: 6.33e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907119810  15 LLEAG-VSVNVPTPEGQTPLMLASSCGNESIAYFLLQQGAELEMKDIHGWTAL 66
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
SAM_sec23ip cd09584
SAM domain of sec23ip; SAM (sterile alpha motif) domain of Sec23ip (Sec23 interacting protein) ...
 355-404 8.28e-07

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: 46.73  E-value: 8.28e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1907119810 355 DLATLLEQIGCLKYLQVFEEQDIDLRIFLTLTESDLKEIGITLfGPKRKM 404
Cdd:cd09584    11 SLQSVLEALSLSEYKSTFEKEKIDMESLLMCTVDDLKEMGIPL-GPRKKI 59
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 11-136 1.45e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 51.22  E-value: 1.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907119810  11 IVHLLLEAGVSVNVPTPEGQTPLMLASSCG--NESIAYfLLQQGAELEMKDIHGWTALFHCTSAG-HQQMVKFLLESGAN 87
Cdd:PHA02876  289 LVPKLLERGADVNAKNIKGETPLYLMAKNGydTENIRT-LIMLGADVNAADRLYITPLHQASTLDrNKDIVITLLELGAN 367

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1907119810  88 ANVREpVYGYTPLMEAAASGHEIIVQYFLNHGVKVDTRDHSGATACMLA 136
Cdd:PHA02876  368 VNARD-YCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFA 415
Ank_2 pfam12796
Ankyrin repeats (3 copies);
100-148 1.78e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 46.26  E-value: 1.78e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1907119810 100 LMEAAASGHEIIVQYFLNHGVKVDTRDHSGATACMLARQFGHMKIVALM 148
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 ...
 353-408 2.17e-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: 2.17e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907119810 353 PQDLATLLEQIGCLKYL-QVFEEQDIDLRIFLTLTESDLKEIGITLFGPKRKMTSAI 408
Cdd:cd09535     5 PEQVAEWLLSAGFDDSVcEKFRENEITGDILLELDLEDLKELDIGSFGKRFKLWNEI 61
Ank_4 pfam13637
Ankyrin repeats (many copies);
96-148 2.18e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.96  E-value: 2.18e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907119810  96 GYTPLMEAAASGHEIIVQYFLNHGVKVDTRDHSGATACMLARQFGHMKIVALM 148
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 2-100 2.39e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 50.26  E-value: 2.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907119810   2 YASYIGHDTIVHLLLEAGVSVNVPTPEGQTPLMLASSCGNESIAYFLLQQGAELEMKDIHGWTAL-FHCTSAGHQQMVKF 80
Cdd:PHA02878  174 YATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLhISVGYCKDYDILKL 253

                          90       100
                  ....*....|....*....|
gi 1907119810  81 LLESGANANVREPVYGYTPL 100
Cdd:PHA02878  254 LLEHGVDVNAKSYILGLTAL 273
Ank_4 pfam13637
Ankyrin repeats (many copies);
31-82 4.59e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.80  E-value: 4.59e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907119810  31 TPLMLASSCGNESIAYFLLQQGAELEMKDIHGWTALFHCTSAGHQQMVKFLL 82
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 11-119 5.91e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 48.83  E-value: 5.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907119810  11 IVHLLLEAGVSVNVPTPEGQTPLMLASSCGNESIAYFLLQQGAELEMKDIHGWTALFHCTSAGHQQMVKFLLESGANANV 90
Cdd:PHA02875  117 IMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDY 196

                          90       100
                  ....*....|....*....|....*....
gi 1907119810  91 REPVYGYTPLMEAAASGHEIIVQYFLNHG 119
Cdd:PHA02875  197 FGKNGCVAALCYAIENNKIDIVRLFIKRG 225
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 6-152 7.07e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 48.81  E-value: 7.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907119810   6 IGHDTIVHLLLEAGVSVNV-PTPegqtplmlassCGNESIAYFLLQQGAELEMKDIHGWTALFHCTSAGHQQMVKFLLES 84
Cdd:PHA02874   78 IGAHDIIKLLIDNGVDTSIlPIP-----------CIEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEY 146

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907119810  85 GANANVREpVYGYTPLMEAAASGHEIIVQYFLNHGVKVDTRDHSGATACMLARQFGHMKIVALMETHS 152
Cdd:PHA02874  147 GADVNIED-DNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHG 213
SAM_caskin1,2_repeat2 cd09498
SAM domain of caskin protein repeat 2; SAM (sterile alpha motif) domain repeat 2 of caskin1,2 ...
 353-410 7.09e-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: 7.09e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907119810 353 PQDLATLLEQIGCLKYLQVFEEQDID-LRIFLTLTESDLKEIGITLFGPKRKMTSAIAR 410
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 ...
 351-408 7.29e-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: 43.74  E-value: 7.29e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907119810 351 SGPQDLATLLEQIGCLKYLQVFEEQDIDLRIFLTLTESDLKEIGITLFGPKRKMTSAI 408
Cdd:cd09534     1 WDEEFVEEWLNELNCGQYLDIFEKNLITGDLLLELDKEALKELGITKVGDRIRLLRAI 58
PHA02798 PHA02798
ankyrin-like protein; Provisional
 11-100 8.08e-06

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 48.68  E-value: 8.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907119810  11 IVHLLLEAGVSVNVPTPEGQTPL--MLASS-CGNESIAYFLLQQGAELEMKDIHGWTALFHCTSAGHQ---QMVKFLLES 84
Cdd:PHA02798   91 IVKILIENGADINKKNSDGETPLycLLSNGyINNLEILLFMIENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEK 170

                          90
                  ....*....|....*.
gi 1907119810  85 GANANVREPVYGYTPL 100
Cdd:PHA02798  171 GVDINTHNNKEKYDTL 186
Ank_4 pfam13637
Ankyrin repeats (many copies);
2-49 1.78e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.26  E-value: 1.78e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1907119810   2 YASYIGHDTIVHLLLEAGVSVNVPTPEGQTPLMLASSCGNESIAYFLL 49
Cdd:pfam13637   7 AAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 44-131 2.34e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 47.18  E-value: 2.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907119810  44 IAYFLLQQGAELEMKDIH-GWTALFHCTSAGHQQMVKFLLESGANANVREPVYGYtPLMEAAASGHEIIVQYFLNHGVKV 122
Cdd:PHA02878  149 ITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNS-PLHHAVKHYNKPIVHILLENGAST 227


                  ....*....
gi 1907119810 123 DTRDHSGAT 131
Cdd:PHA02878  228 DARDKCGNT 236
SAM_DDHD2 cd09585
SAM domain of DDHD2; SAM (sterile alpha motif) domain of DDHD2 group is a potential ...
 356-410 2.86e-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: 42.05  E-value: 2.86e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1907119810 356 LATLLEQIGCLKYLQVFEEQDIDLRIFLTLTESDLKEIGITLfGPKRKMTSAIAR 410
Cdd:cd09585    12 LEETLKKLGLSEYCDVFEKEKIDLEALALCQERDLKDLGIPL-GPRKKILNYIRR 65
PHA03095 PHA03095
ankyrin-like protein; Provisional
 11-154 3.50e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 46.56  E-value: 3.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907119810  11 IVHLLLEAGVSVNVPTPEGQTPL--MLASSCGNESIAYFLLQQGAELEMKDIHGWTALFHC---TSAGHQQMVKFLlESG 85
Cdd:PHA03095  169 LLRLLIDAGADVYAVDDRFRSLLhhHLQSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMatgSSCKRSLVLPLL-IAG 247

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907119810  86 ANANVREpVYGYTPLMEAAASGHEIIVQYFLNHGVKVDTRDHSGATACMLARQFGHMKIV-ALMETHSPV 154
Cdd:PHA03095  248 ISINARN-RYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVrAALAKNPSA 316
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 2-103 4.68e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 46.11  E-value: 4.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907119810   2 YASYIGHDTIVHLLLEAGVSVNVPTPEGQTPLMLASSCGNESIAYFLLQQGAELEMKDIHGWTALFHCTSAGHQQMVKFL 81
Cdd:PHA02874  130 YAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLL 209

                          90       100
                  ....*....|....*....|..
gi 1907119810  82 LESGANANVREPvYGYTPLMEA 103
Cdd:PHA02874  210 IDHGNHIMNKCK-NGFTPLHNA 230
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 95-124 5.52e-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: 5.52e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 1907119810  95 YGYTPLMEAAASGHEIIVQYFLNHGVKVDT 124
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
SAM_ASZ1 cd09521
SAM domain of ASZ1 subfamily; SAM (sterile alpha motif) domain of ASZ1 (Ankyrin, SAM, leucine ...
 350-412 6.43e-05

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: 41.12  E-value: 6.43e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907119810 350 YSGPQDLATLLEQIGCLKYLQVFEEQDIDLRIFLTLTESDLKEIGITLFGPKRKMTSAIARWH 412
Cdd:cd09521     2 YSKLDDLELFLHGLELGHLTPLFKEHDVTFSQLLKMTEEDLEKIGITQPGDQKKILDAIKEVH 64
SAM_DGK-delta-eta cd09507
SAM domain of diacylglycerol kinase delta and eta subunits; SAM (sterile alpha motif) domain ...
 349-409 6.60e-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: 41.24  E-value: 6.60e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907119810 349 PYSGPQDLATLLEQIGCLKYLQVFEEQDIDLRIFLTLTESDLKEIGITLFGPKRKMTSAIA 409
Cdd:cd09507     3 TNWTTEEVGAWLESLQLGEYRDIFARNDIRGSELLHLERRDLKDLGITKVGHVKRILQAIK 63
Ank_5 pfam13857
Ankyrin repeats (many copies);
81-132 8.84e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.41  E-value: 8.84e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907119810  81 LLESGANANVREPVYGYTPLMEAAASGHEIIVQYFLNHGVKVDTRDHSGATA 132
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTA 52
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 95-127 9.28e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 39.58  E-value: 9.28e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1907119810  95 YGYTPLMEAAAS-GHEIIVQYFLNHGVKVDTRDH 127
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
SAM_TAL cd09523
SAM domain of TAL subfamily; SAM (sterile alpha motif) domain of TAL (Tsg101-associated ligase) ...
 355-412 9.95e-05

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: 40.73  E-value: 9.95e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907119810 355 DLATLLEQIGCLKYLQVFEEQDIDLRIFLTLTESDLKEIGITLFGPKRKMTSAIARWH 412
Cdd:cd09523     7 QLVNLLNELSAEHYLPVFARHRITMETLSTMTDEDLKKIGIHEIGLRKEILRAAQELL 64
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 95-123 1.20e-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: 1.20e-04
                           10        20
                   ....*....|....*....|....*....
gi 1907119810   95 YGYTPLMEAAASGHEIIVQYFLNHGVKVD 123
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 61-91 1.20e-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: 1.20e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1907119810  61 HGWTALFH-CTSAGHQQMVKFLLESGANANVR 91
Cdd:pfam00023   1 DGNTPLHLaAGRRGNLEIVKLLLSKGADVNAR 32
PHA03095 PHA03095
ankyrin-like protein; Provisional
 48-132 1.29e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 44.63  E-value: 1.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907119810  48 LLQQGAELEMKDIHGWTALFHCTSAGHQQ---MVKFLLESGANANVREpVYGYTPLMEAAASGHEI-IVQYFLNHGVKVD 123
Cdd:PHA03095   33 LLAAGADVNFRGEYGKTPLHLYLHYSSEKvkdIVRLLLEAGADVNAPE-RCGFTPLHLYLYNATTLdVIKLLIKAGADVN 111


                  ....*....
gi 1907119810 124 TRDHSGATA 132
Cdd:PHA03095  112 AKDKVGRTP 120
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 66-178 3.07e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 43.73  E-value: 3.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907119810  66 LFHCTSAGHQQMVKFLLESGANANVREpVYGYTPLMEAAASGHEIIVQYFLNHGVKVDTRDHSGATACMLARQFGHMKIV 145
Cdd:PTZ00322   86 LCQLAASGDAVGARILLTGGADPNCRD-YDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVV 164

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1907119810 146 ALMETHSPVLPKSLYRS-PEKYEDLSSSDESWPV 178
Cdd:PTZ00322  165 QLLSRHSQCHFELGANAkPDSFTGKPPSLEDSPI 198
SAM_tankyrase1,2 cd09524
SAM domain of tankyrase1,2 subfamily; SAM (sterile alpha motif) domain of Tankyrase1,2 ...
 355-410 7.37e-04

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: 38.08  E-value: 7.37e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907119810 355 DLATLLEQIGCLKYLQVFEEQDIDLRIFLTLTESDLKEIGITLFGPKRKMTSAIAR 410
Cdd:cd09524     7 SISQFLSSLGLEHLREIFEREQITLDVLAEMGHEELKEIGINAYGHRHKLIKGVER 62
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 28-59 1.02e-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: 36.88  E-value: 1.02e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1907119810  28 EGQTPLMLAS-SCGNESIAYFLLQQGAELEMKD 59
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 35-139 1.73e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 41.42  E-value: 1.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907119810  35 LASScGNESIAYFLLQQGAELEMKDIHGWTALFHCTSAGHQQMVKFLLESGANANV--REpvyGYTPLMEAAASGHEIIV 112
Cdd:PTZ00322   89 LAAS-GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLldKD---GKTPLELAEENGFREVV 164

                          90       100
                  ....*....|....*....|....*..
gi 1907119810 113 QYFLNHgvkvdTRDHSGATACMLARQF 139
Cdd:PTZ00322  165 QLLSRH-----SQCHFELGANAKPDSF 186
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 61-90 2.15e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 35.64  E-value: 2.15e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1907119810   61 HGWTALFHCTSAGHQQMVKFLLESGANANV 90
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02791 PHA02791
ankyrin-like protein; Provisional
 59-147 2.41e-03

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 40.03  E-value: 2.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907119810  59 DIHGWTALFHCTSAGHQQMVKFLLESGANANVREPVYgytPLMEAAASGHEIIVQYFLNHGVKVDTRDHSGATACMLARQ 138
Cdd:PHA02791   27 DVHGHSALYYAIADNNVRLVCTLLNAGALKNLLENEF---PLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVD 103


                  ....*....
gi 1907119810 139 FGHMKIVAL 147
Cdd:PHA02791  104 SGNMQTVKL 112
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 10-117 2.60e-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: 40.77  E-value: 2.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907119810  10 TIVHLLLEAGVSVNVPTPEG--------------QTPLMLASSCGNESIAYFLLQQGAELEMKDIHGWTALFHCTSAGHQ 75
Cdd:cd22192   103 NLVRELIARGADVVSPRATGtffrpgpknliyygEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNK 182

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907119810  76 ----QMVKFLLESGANANvREPVY------GYTPLMEAAASGHEIIVQYFLN 117
Cdd:cd22192   183 tfacQMYDLILSYDKEDD-LQPLDlvpnnqGLTPFKLAAKEGNIVMFQHLVQ 233
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 11-126 4.89e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 39.72  E-value: 4.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907119810  11 IVHLLLEAGVSVNVPTPEGQTPLM---LASSCGNESIAYFLLQQGAEL-EMKDIHGWTaLFHCTSAG---HQQMVKFLLE 83
Cdd:PHA02989   90 IVKLLLKFGADINLKTFNGVSPIVcfiYNSNINNCDMLRFLLSKGINVnDVKNSRGYN-LLHMYLESfsvKKDVIKILLS 168

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1907119810  84 SGANANVREPVYGYTPL---MEAAASGHEI-IVQYFLNHGVKVDTRD 126
Cdd:PHA02989  169 FGVNLFEKTSLYGLTPMniyLRNDIDVISIkVIKYLIKKGVNIETNN 215
Ank_5 pfam13857
Ankyrin repeats (many copies);
1-36 5.26e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.40  E-value: 5.26e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1907119810   1 MYASYIGHDTIVHLLLEAGVSVNVPTPEGQTPLMLA 36
Cdd:pfam13857  21 HVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02946 PHA02946
ankyin-like protein; Provisional
 9-129 5.33e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 39.65  E-value: 5.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907119810   9 DTIVHLLLEAGVSVNVPTPEGQTPLMLASSCGNESIAYFLLQQGAELEMKDIHGWTALFHCTSAGHQ--QMVKFLLESGA 86
Cdd:PHA02946   52 ERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEviERINLLVQYGA 131

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1907119810  87 NANVREPVYGYTPLMeAAASGHEIIVQYFLNHGVKVDTRDHSG 129
Cdd:PHA02946  132 KINNSVDEEGCGPLL-ACTDPSERVFKKIMSIGFEARIVDKFG 173
SAM_HARP cd09587
SAM domain of HARP subfamily; SAM (sterile alpha motif) domain of HARP (Harmonin-interacting ...
 356-418 5.38e-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: 5.38e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907119810 356 LATLLEQIGCLKYLQVFEEQDIDLRIFLTLTESDLKEIGITLfGPKRKMTSAIARWHSSARPP 418
Cdd:cd09587     5 LEVFLSSQHLEEFLPIFMREQIDLEALMLCSDEDLQNIQMQL-GPRKKILSAVARRKQVLQQP 66
SAM_SARM1-like_repeat1 cd09501
SAM domain ot SARM1-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 355-410 5.44e-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: 5.44e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907119810 355 DLATLLEQIGCLKYLQVFEEQDIDLRIFLTLTESDLKE-IGitlfgpkrkMTSAIAR 410
Cdd:cd09501     8 DVQTWLKQIGFEDYAEKFSESQVDGDLLLQLTEDELKQdLG---------MSSGLLR 55
SAM_Polycomb cd09509
SAM domain of Polycomb group; SAM (sterile alpha motif) domain of Polycomb group is a ...
 364-410 6.08e-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: 6.08e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1907119810 364 GCLKYLQVFEEQDIDLRIFLTLTESDL-KEIGITLfGPKRKMTSAIAR 410
Cdd:cd09509    18 GCAEYAEVFREQEIDGQALLLLTEDDLlKGMGLKL-GPALKIYNHIVK 64
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 28-57 7.20e-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: 7.20e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1907119810   28 EGQTPLMLASSCGNESIAYFLLQQGAELEM 57
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 28-57 7.81e-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: 7.81e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1907119810  28 EGQTPLMLASSCGNESIAYFLLQQGAELEM 57
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
SAM_Scm-like-3MBT3,4 cd09582
SAM domain of Scm-like-3MBT3,4 proteins of Polycomb group; SAM (sterile alpha motif) domain of ...
 364-412 9.58e-03

SAM domain of Scm-like-3MBT3,4 proteins of Polycomb group; SAM (sterile alpha motif) domain of Scm-like-3MBT3,4 (Sex comb on midleg, Malignant brain tumor) subfamily proteins (also known as L3mbtl3,4 proteins) is a putative protein-protein interaction domain. Proteins of this subfamily are predicted transcriptional regulators belonging to Polycomb group. The majority of them are multidomain proteins: in addition to the C-terminal SAM domain, they contain three MBT repeats and Zn finger domain. Murine L3mbtl3 protein of this subfamily is essential for maturation of myeloid progenitor cells during differentiation. Human L3mbtl4 is a potential tumor suppressor gene in breast cancer, while deregulation of L3MBTL3 is associated with neuroblastoma.


Pssm-ID: 188981  Cd Length: 66  Bit Score: 34.94  E-value: 9.58e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1907119810 364 GCLKYLQVFEEQDIDLRIFLTLTESDLKEI-GITLfGPKRKMTSAIARWH 412
Cdd:cd09582    18 GCEEHAKVFRDEQIDGEAFLLLTQSDLVKIlGIKL-GPALKIYNSILMLR 66
 
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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