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Conserved domains on  [gi|1720387813|ref|XP_030105150|]
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ankyrin repeat and SAM domain-containing protein 3 isoform X9 [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
SAM_ANKS3 cd09519
SAM domain of ANKS3 subfamily; SAM (sterile alpha motif) domain of ANKS3 subfamily is a ...
 362-425 4.59e-38

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: 134.16  E-value: 4.59e-38
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720387813 362 YSGPQDLATLLEQIGCLKYLQVFEEQDIDLRIFLTLTESDLKEIGITLFGPKRKMTSAIARWHS 425
Cdd:cd09519     1 YTGPKDLSELLEQIGCSKYLPIFEEQDIDLRIFLTLTESDLKEIGITLFGPKRKMTSAIARWHS 64
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
62-159 7.67e-26

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 107.73  E-value: 7.67e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387813  62 KQGAELEMKDIHGWTALFHCTSAGHQQMVKFLLESGANANVREPvYGYTPLMEAAASGHEIIVQYFLNHGVKVDTRDHSG 141
Cdd:COG0666   108 EAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDN-DGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDG 186

                          90
                  ....*....|....*...
gi 1720387813 142 ATACMLARQFGHMKIVAL 159
Cdd:COG0666   187 ETPLHLAAENGHLEIVKL 204
 
Name Accession Description Interval E-value
SAM_ANKS3 cd09519
SAM domain of ANKS3 subfamily; SAM (sterile alpha motif) domain of ANKS3 subfamily is a ...
 362-425 4.59e-38

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: 134.16  E-value: 4.59e-38
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720387813 362 YSGPQDLATLLEQIGCLKYLQVFEEQDIDLRIFLTLTESDLKEIGITLFGPKRKMTSAIARWHS 425
Cdd:cd09519     1 YTGPKDLSELLEQIGCSKYLPIFEEQDIDLRIFLTLTESDLKEIGITLFGPKRKMTSAIARWHS 64
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
62-159 7.67e-26

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 107.73  E-value: 7.67e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387813  62 KQGAELEMKDIHGWTALFHCTSAGHQQMVKFLLESGANANVREPvYGYTPLMEAAASGHEIIVQYFLNHGVKVDTRDHSG 141
Cdd:COG0666   108 EAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDN-DGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDG 186

                          90
                  ....*....|....*...
gi 1720387813 142 ATACMLARQFGHMKIVAL 159
Cdd:COG0666   187 ETPLHLAAENGHLEIVKL 204
Ank_2 pfam12796
Ankyrin repeats (3 copies);
62-138 1.91e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 74.77  E-value: 1.91e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720387813  62 KQGAELEMKDIHGWTALFHCTSAGHQQMVKFLLEsgaNANVREPVYGYTPLMEAAASGHEIIVQYFLNHGVKVDTRD 138
Cdd:pfam12796  18 ENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE---HADVNLKDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 362-423 1.99e-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: 59.59  E-value: 1.99e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720387813 362 YSGPQDLATLLEQIGCLKYLQVFEEQDIDLRIFLTLTESDLKEIGITLFGPKRKMTSAIARW 423
Cdd:pfam00536   2 GWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLKLGVTLLGHRKKILYAIQRL 63
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 361-420 7.29e-11

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: 58.08  E-value: 7.29e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720387813  361 PYSGPQDLATLLEQIGCLKYLQVFEEQDIDLRIFLTLT-ESDLKEIGITLFGPKRKMTSAI 420
Cdd:smart00454   2 SQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTsEEDLKELGITKLGHRKKILKAI 62
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 16-185 1.17e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 61.42  E-value: 1.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387813  16 NRTSVTFPGCSAPCEDYFRGGPGAGLSAGEGRAAVAGGWPGNLRPC-----KQGAELEMKDIHGWTALFHCTSAGHQQMV 90
Cdd:PLN03192  528 NLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCvlvllKHACNVHIRDANGNTALWNAISAKHHKIF 607

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387813  91 KFLLESganANVREPVYGYTPLMEAAASGHEIIVQYFLNHGVKVDTRDHSGATACMLARQFGHMKIVALMETHSPVLPKS 170
Cdd:PLN03192  608 RILYHF---ASISDPHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKA 684

                         170
                  ....*....|....*
gi 1720387813 171 lyrspEKYEDLSSSD 185
Cdd:PLN03192  685 -----NTDDDFSPTE 694
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 107-135 1.18e-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: 1.18e-04
                           10        20
                   ....*....|....*....|....*....
gi 1720387813  107 YGYTPLMEAAASGHEIIVQYFLNHGVKVD 135
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
 
Name Accession Description Interval E-value
SAM_ANKS3 cd09519
SAM domain of ANKS3 subfamily; SAM (sterile alpha motif) domain of ANKS3 subfamily is a ...
 362-425 4.59e-38

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: 134.16  E-value: 4.59e-38
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720387813 362 YSGPQDLATLLEQIGCLKYLQVFEEQDIDLRIFLTLTESDLKEIGITLFGPKRKMTSAIARWHS 425
Cdd:cd09519     1 YTGPKDLSELLEQIGCSKYLPIFEEQDIDLRIFLTLTESDLKEIGITLFGPKRKMTSAIARWHS 64
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
62-159 7.67e-26

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 107.73  E-value: 7.67e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387813  62 KQGAELEMKDIHGWTALFHCTSAGHQQMVKFLLESGANANVREPvYGYTPLMEAAASGHEIIVQYFLNHGVKVDTRDHSG 141
Cdd:COG0666   108 EAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDN-DGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDG 186

                          90
                  ....*....|....*...
gi 1720387813 142 ATACMLARQFGHMKIVAL 159
Cdd:COG0666   187 ETPLHLAAENGHLEIVKL 204
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
62-163 1.50e-24

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 103.88  E-value: 1.50e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387813  62 KQGAELEMKDIHGWTALFHCTSAGHQQMVKFLLESGANANVREPvYGYTPLMEAAASGHEIIVQYFLNHGVKVDTRDHSG 141
Cdd:COG0666   141 EAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDN-DGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDG 219

                          90       100
                  ....*....|....*....|..
gi 1720387813 142 ATACMLARQFGHMKIVALMETH 163
Cdd:COG0666   220 KTALDLAAENGNLEIVKLLLEA 241
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
62-160 3.55e-21

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 93.87  E-value: 3.55e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387813  62 KQGAELEMKDIHGWTALFHCTSAGHQQMVKFLLESGANANVREPvYGYTPLMEAAASGHEIIVQYFLNHGVKVDTRDHSG 141
Cdd:COG0666    75 AAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDK-DGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDG 153

                          90
                  ....*....|....*....
gi 1720387813 142 ATACMLARQFGHMKIVALM 160
Cdd:COG0666   154 NTPLHLAAANGNLEIVKLL 172
SAM_BICC1 cd09520
SAM domain of BICC1 (bicaudal) subfamily; SAM (sterile alpha motif) domain of BICC1 (bicaudal) ...
 362-421 2.17e-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: 2.17e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387813 362 YSGPQDLATLLEQIGCLKYLQVFEEQDIDLRIFLTLTESDLKEIGITLFGPKRKMTSAIA 421
Cdd:cd09520     1 SAKYSDLPELLAKLGLEKYIDLFAQQEIDLQTFLTLTDQDLKELGITAFGARRKMLLAIS 60
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
62-160 9.15e-17

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 81.15  E-value: 9.15e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387813  62 KQGAELEMKDIHGWTALFHCTSAGHQQMVKFLLESGANANVREPvYGYTPLMEAAASGHEIIVQYFLNHGVKVDTRDHSG 141
Cdd:COG0666   174 EAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDN-DGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDG 252

                          90
                  ....*....|....*....
gi 1720387813 142 ATACMLARQFGHMKIVALM 160
Cdd:COG0666   253 LTALLLAAAAGAALIVKLL 271
Ank_2 pfam12796
Ankyrin repeats (3 copies);
62-138 1.91e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 74.77  E-value: 1.91e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720387813  62 KQGAELEMKDIHGWTALFHCTSAGHQQMVKFLLEsgaNANVREPVYGYTPLMEAAASGHEIIVQYFLNHGVKVDTRD 138
Cdd:pfam12796  18 ENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE---HADVNLKDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 367-422 1.76e-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: 68.03  E-value: 1.76e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720387813 367 DLATLLEQIGCLKYLQVFEEQDIDLRIFLTLTESDLKEIGITLFGPKRKMTSAIAR 422
Cdd:cd09487     1 DVAEWLESLGLEQYADLFRKNEIDGDALLLLTDEDLKELGITSPGHRKKILRAIQR 56
Ank_2 pfam12796
Ankyrin repeats (3 copies);
78-157 2.79e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 65.52  E-value: 2.79e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387813  78 LFHCTSAGHQQMVKFLLESGANANVREPvYGYTPLMEAAASGHEIIVQYFLNHgVKVDTRDHsGATACMLARQFGHMKIV 157
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDK-NGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIV 77
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 362-423 1.99e-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: 59.59  E-value: 1.99e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720387813 362 YSGPQDLATLLEQIGCLKYLQVFEEQDIDLRIFLTLTESDLKEIGITLFGPKRKMTSAIARW 423
Cdd:pfam00536   2 GWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLKLGVTLLGHRKKILYAIQRL 63
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
70-159 2.23e-11

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 64.98  E-value: 2.23e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387813  70 KDIHGWTALFHCTSAGHQQMVKFLLESGANANVREPvYGYTPLMEAAASGHEIIVQYFLNHGVKVDTRDHSGATACMLAR 149
Cdd:COG0666    50 ADALGALLLLAAALAGDLLVALLLLAAGADINAKDD-GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAA 128

                          90
                  ....*....|
gi 1720387813 150 QFGHMKIVAL 159
Cdd:COG0666   129 YNGNLEIVKL 138
SAM_ANKS6 cd09518
SAM domain of ANKS6 (or SamCystin) subfamily; SAM (sterile alpha motif) domain of ANKS6 (or ...
 367-425 5.21e-11

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: 58.35  E-value: 5.21e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720387813 367 DLATLLEQIGCLKYLQVFEEQDIDLRIFLTLTESDLKEIGITLFGPKRKMTSAIARWHS 425
Cdd:cd09518     7 ELSGILRKLSLEKYQPIFEEQEVDMEAFLTLTDGDLKELGIKTDGPRQQILAAISELNA 65
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 361-420 7.29e-11

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: 58.08  E-value: 7.29e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720387813  361 PYSGPQDLATLLEQIGCLKYLQVFEEQDIDLRIFLTLT-ESDLKEIGITLFGPKRKMTSAI 420
Cdd:smart00454   2 SQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTsEEDLKELGITKLGHRKKILKAI 62
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
361-420 1.14e-09

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 54.58  E-value: 1.14e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720387813 361 PYSGPQDLATLLEQIGCLKYLQVFEEQDID-LRIFLTLTESDLKEIGITLFGPKRKMTSAI 420
Cdd:pfam07647   2 ESWSLESVADWLRSIGLEQYTDNFRDQGITgAELLLRLTLEDLKRLGITSVGHRRKILKKI 62
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 16-185 1.17e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 61.42  E-value: 1.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387813  16 NRTSVTFPGCSAPCEDYFRGGPGAGLSAGEGRAAVAGGWPGNLRPC-----KQGAELEMKDIHGWTALFHCTSAGHQQMV 90
Cdd:PLN03192  528 NLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCvlvllKHACNVHIRDANGNTALWNAISAKHHKIF 607

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387813  91 KFLLESganANVREPVYGYTPLMEAAASGHEIIVQYFLNHGVKVDTRDHSGATACMLARQFGHMKIVALMETHSPVLPKS 170
Cdd:PLN03192  608 RILYHF---ASISDPHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKA 684

                         170
                  ....*....|....*
gi 1720387813 171 lyrspEKYEDLSSSD 185
Cdd:PLN03192  685 -----NTDDDFSPTE 694
SAM_sec23ip-like cd09516
SAM domain of sec23ip-like subfamily; SAM (sterile alpha motif) domain of Sec23ip-like (Sec23 ...
 365-416 1.30e-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: 54.34  E-value: 1.30e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1720387813 365 PQDLATLLEQIGCLKYLQVFEEQDIDLRIFLTLTESDLKEIGITLfGPKRKM 416
Cdd:cd09516     9 PLTLEEDLEKLGLSEYFDTFEKEKIDMESLLLCSESDLKEMGIPM-GPRKKL 59
Ank_4 pfam13637
Ankyrin repeats (many copies);
74-128 3.64e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.66  E-value: 3.64e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1720387813  74 GWTALFHCTSAGHQQMVKFLLESGANANVRePVYGYTPLMEAAASGHEIIVQYFL 128
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAV-DGNGETALHFAASNGNVEVLKLLL 54
SAM_USH1G_HARP cd09517
SAM domain of USH1G_HARP family; SAM (sterile alpha motif) domain of USH1G/HARP (Usher ...
 368-422 5.21e-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: 50.03  E-value: 5.21e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1720387813 368 LATLLEQIGCLKYLQVFEEQDIDLRIFLTLTESDLKEIGITLfGPKRKMTSAIAR 422
Cdd:cd09517     5 LERFLTSNHLEEYLPVFEREKIDLEALMLLTDEDLQSLKLPL-GPRRKLLNAIAK 58
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 70-136 9.01e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 54.67  E-value: 9.01e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720387813  70 KDIHGWTALFHCTSAGHQQMVKFLLESGANANVREpVYGYTPLMEAAASGHEIIVQYFLNHGVKVDT 136
Cdd:PHA03100  188 KDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVN-KYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
SAM_sec23ip cd09584
SAM domain of sec23ip; SAM (sterile alpha motif) domain of Sec23ip (Sec23 interacting protein) ...
 367-416 3.58e-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: 47.50  E-value: 3.58e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1720387813 367 DLATLLEQIGCLKYLQVFEEQDIDLRIFLTLTESDLKEIGITLfGPKRKM 416
Cdd:cd09584    11 SLQSVLEALSLSEYKSTFEKEKIDMESLLMCTVDDLKEMGIPL-GPRKKI 59
Ank_4 pfam13637
Ankyrin repeats (many copies);
108-160 1.71e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.34  E-value: 1.71e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1720387813 108 GYTPLMEAAASGHEIIVQYFLNHGVKVDTRDHSGATACMLARQFGHMKIVALM 160
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
Ank_2 pfam12796
Ankyrin repeats (3 copies);
112-160 1.76e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 46.26  E-value: 1.76e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1720387813 112 LMEAAASGHEIIVQYFLNHGVKVDTRDHSGATACMLARQFGHMKIVALM 160
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 ...
 365-420 2.14e-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: 2.14e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720387813 365 PQDLATLLEQIGCLKYL-QVFEEQDIDLRIFLTLTESDLKEIGITLFGPKRKMTSAI 420
Cdd:cd09535     5 PEQVAEWLLSAGFDDSVcEKFRENEITGDILLELDLEDLKELDIGSFGKRFKLWNEI 61
SAM_caskin1,2_repeat2 cd09498
SAM domain of caskin protein repeat 2; SAM (sterile alpha motif) domain repeat 2 of caskin1,2 ...
 365-422 5.36e-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: 44.21  E-value: 5.36e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720387813 365 PQDLATLLEQIGCLKYLQVFEEQDID-LRIFLTLTESDLKEIGITLFGPKRKMTSAIAR 422
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 ...
 363-420 7.18e-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: 7.18e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720387813 363 SGPQDLATLLEQIGCLKYLQVFEEQDIDLRIFLTLTESDLKEIGITLFGPKRKMTSAI 420
Cdd:cd09534     1 WDEEFVEEWLNELNCGQYLDIFEKNLITGDLLLELDKEALKELGITKVGDRIRLLRAI 58
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
62-144 1.02e-05

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 47.64  E-value: 1.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387813  62 KQGAELEMKDIHGWTALFHCTSAGHQQMVKFLLESGANANVREPvYGYTPLMEAAASGHEIIVQYFLNHGVKVDTRDHSG 141
Cdd:COG0666   207 EAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDK-DGLTALLLAAAAGAALIVKLLLLALLLLAAALLDL 285


                  ...
gi 1720387813 142 ATA 144
Cdd:COG0666   286 LTL 288
SAM_DDHD2 cd09585
SAM domain of DDHD2; SAM (sterile alpha motif) domain of DDHD2 group is a potential ...
 368-422 1.76e-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: 42.82  E-value: 1.76e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1720387813 368 LATLLEQIGCLKYLQVFEEQDIDLRIFLTLTESDLKEIGITLfGPKRKMTSAIAR 422
Cdd:cd09585    12 LEETLKKLGLSEYCDVFEKEKIDLEALALCQERDLKDLGIPL-GPRKKILNYIRR 65
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 62-157 2.51e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 46.97  E-value: 2.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387813  62 KQGAELEMKDIHGWTALFHC--TSAGHQQMVKFLLESGANANVREPvYGYTPLMEAAASGH---EII------------- 123
Cdd:PHA03100   94 EYGANVNAPDNNGITPLLYAisKKSNSYSIVEYLLDNGANVNIKNS-DGENLLHLYLESNKidlKILkllidkgvdinak 172

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1720387813 124 --VQYFLNHGVKVDTRDHSGATACMLARQFGHMKIV 157
Cdd:PHA03100  173 nrVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFV 208
SAM_ASZ1 cd09521
SAM domain of ASZ1 subfamily; SAM (sterile alpha motif) domain of ASZ1 (Ankyrin, SAM, leucine ...
 362-424 2.97e-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: 41.89  E-value: 2.97e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720387813 362 YSGPQDLATLLEQIGCLKYLQVFEEQDIDLRIFLTLTESDLKEIGITLFGPKRKMTSAIARWH 424
Cdd:cd09521     2 YSKLDDLELFLHGLELGHLTPLFKEHDVTFSQLLKMTEEDLEKIGITQPGDQKKILDAIKEVH 64
SAM_TAL cd09523
SAM domain of TAL subfamily; SAM (sterile alpha motif) domain of TAL (Tsg101-associated ligase) ...
 367-424 4.79e-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: 41.50  E-value: 4.79e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720387813 367 DLATLLEQIGCLKYLQVFEEQDIDLRIFLTLTESDLKEIGITLFGPKRKMTSAIARWH 424
Cdd:cd09523     7 QLVNLLNELSAEHYLPVFARHRITMETLSTMTDEDLKKIGIHEIGLRKEILRAAQELL 64
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 107-136 5.44e-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: 5.44e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 1720387813 107 YGYTPLMEAAASGHEIIVQYFLNHGVKVDT 136
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 62-143 6.17e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 45.72  E-value: 6.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387813  62 KQGAELEMKDIHGWTALFHCTSAGHQQMVKFLLESGANANVREpVYGYTPLMEAAASGHEIIVQYFLNHGVKVDTRDHSG 141
Cdd:PHA02874  145 EYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKD-NNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNG 223


                  ..
gi 1720387813 142 AT 143
Cdd:PHA02874  224 FT 225
SAM_DGK-delta-eta cd09507
SAM domain of diacylglycerol kinase delta and eta subunits; SAM (sterile alpha motif) domain ...
 361-421 6.50e-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: 6.50e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720387813 361 PYSGPQDLATLLEQIGCLKYLQVFEEQDIDLRIFLTLTESDLKEIGITLFGPKRKMTSAIA 421
Cdd:cd09507     3 TNWTTEEVGAWLESLQLGEYRDIFARNDIRGSELLHLERRDLKDLGITKVGHVKRILQAIK 63
Ank_5 pfam13857
Ankyrin repeats (many copies);
93-144 8.72e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.41  E-value: 8.72e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1720387813  93 LLESGANANVREPVYGYTPLMEAAASGHEIIVQYFLNHGVKVDTRDHSGATA 144
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTA 52
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 107-139 9.15e-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: 9.15e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1720387813 107 YGYTPLMEAAAS-GHEIIVQYFLNHGVKVDTRDH 139
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 107-135 1.18e-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: 1.18e-04
                           10        20
                   ....*....|....*....|....*....
gi 1720387813  107 YGYTPLMEAAASGHEIIVQYFLNHGVKVD 135
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 73-103 1.18e-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: 1.18e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1720387813  73 HGWTALFH-CTSAGHQQMVKFLLESGANANVR 103
Cdd:pfam00023   1 DGNTPLHLaAGRRGNLEIVKLLLSKGADVNAR 32
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 90-143 2.14e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 43.89  E-value: 2.14e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1720387813  90 VKFLLESGANANVREpVYGYTPLMEAAASGHEIIVQYFLNHGVKVDTRDHSGAT 143
Cdd:PHA03100  175 VNYLLSYGVPINIKD-VYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDT 227
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 78-190 2.67e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 43.73  E-value: 2.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387813  78 LFHCTSAGHQQMVKFLLESGANANVREpVYGYTPLMEAAASGHEIIVQYFLNHGVKVDTRDHSGATACMLARQFGHMKIV 157
Cdd:PTZ00322   86 LCQLAASGDAVGARILLTGGADPNCRD-YDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVV 164

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1720387813 158 ALMETHSPVLPKSLYRS-PEKYEDLSSSDESWPV 190
Cdd:PTZ00322  165 QLLSRHSQCHFELGANAkPDSFTGKPPSLEDSPI 198
PHA03095 PHA03095
ankyrin-like protein; Provisional
 64-144 3.19e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 43.47  E-value: 3.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387813  64 GAELEMKDIHGWTALfHC--TSAGHQQMVKFLLESGANANVREpVYGYTPLmEAAASGHEI---IVQYFLNHGVKVDTRD 138
Cdd:PHA03095   73 GADVNAPERCGFTPL-HLylYNATTLDVIKLLIKAGADVNAKD-KVGRTPL-HVYLSGFNInpkVIRLLLRKGADVNALD 149


                  ....*.
gi 1720387813 139 HSGATA 144
Cdd:PHA03095  150 LYGMTP 155
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 64-143 3.68e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 43.33  E-value: 3.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387813  64 GAELEMKDIH-GWTALFHCTSAGHQQMVKFLLESGANANVREPVYGYtPLMEAAASGHEIIVQYFLNHGVKVDTRDHSGA 142
Cdd:PHA02878  157 GADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNS-PLHHAVKHYNKPIVHILLENGASTDARDKCGN 235


                  .
gi 1720387813 143 T 143
Cdd:PHA02878  236 T 236
SAM_tankyrase1,2 cd09524
SAM domain of tankyrase1,2 subfamily; SAM (sterile alpha motif) domain of Tankyrase1,2 ...
 367-422 4.90e-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: 38.46  E-value: 4.90e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720387813 367 DLATLLEQIGCLKYLQVFEEQDIDLRIFLTLTESDLKEIGITLFGPKRKMTSAIAR 422
Cdd:cd09524     7 SISQFLSSLGLEHLREIFEREQITLDVLAEMGHEELKEIGINAYGHRHKLIKGVER 62
PHA03095 PHA03095
ankyrin-like protein; Provisional
 62-144 5.70e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 42.70  E-value: 5.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387813  62 KQGAELEMKDIHGWTALFHCTSAGHQQ---MVKFLLESGANANVREpVYGYTPLMEAAASGHEI-IVQYFLNHGVKVDTR 137
Cdd:PHA03095   35 AAGADVNFRGEYGKTPLHLYLHYSSEKvkdIVRLLLEAGADVNAPE-RCGFTPLHLYLYNATTLdVIKLLIKAGADVNAK 113


                  ....*..
gi 1720387813 138 DHSGATA 144
Cdd:PHA03095  114 DKVGRTP 120
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 73-102 2.12e-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: 2.12e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1720387813   73 HGWTALFHCTSAGHQQMVKFLLESGANANV 102
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02791 PHA02791
ankyrin-like protein; Provisional
 71-159 2.37e-03

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 40.03  E-value: 2.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387813  71 DIHGWTALFHCTSAGHQQMVKFLLESGANANVREPVYgytPLMEAAASGHEIIVQYFLNHGVKVDTRDHSGATACMLARQ 150
Cdd:PHA02791   27 DVHGHSALYYAIADNNVRLVCTLLNAGALKNLLENEF---PLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVD 103


                  ....*....
gi 1720387813 151 FGHMKIVAL 159
Cdd:PHA02791  104 SGNMQTVKL 112
SAM_HARP cd09587
SAM domain of HARP subfamily; SAM (sterile alpha motif) domain of HARP (Harmonin-interacting ...
 368-430 3.27e-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: 36.34  E-value: 3.27e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720387813 368 LATLLEQIGCLKYLQVFEEQDIDLRIFLTLTESDLKEIGITLfGPKRKMTSAIARWHSSARPP 430
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 ...
 367-422 5.37e-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: 5.37e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720387813 367 DLATLLEQIGCLKYLQVFEEQDIDLRIFLTLTESDLKE-IGitlfgpkrkMTSAIAR 422
Cdd:cd09501     8 DVQTWLKQIGFEDYAEKFSESQVDGDLLLQLTEDELKQdLG---------MSSGLLR 55
SAM_Polycomb cd09509
SAM domain of Polycomb group; SAM (sterile alpha motif) domain of Polycomb group is a ...
 376-422 6.00e-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: 6.00e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1720387813 376 GCLKYLQVFEEQDIDLRIFLTLTESDL-KEIGITLfGPKRKMTSAIAR 422
Cdd:cd09509    18 GCAEYAEVFREQEIDGQALLLLTEDDLlKGMGLKL-GPALKIYNHIVK 64
PHA03095 PHA03095
ankyrin-like protein; Provisional
 90-166 6.44e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 39.24  E-value: 6.44e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720387813  90 VKFLLESGANANVREpVYGYTPLMEAAASGHEIIVQYFLNHGVKVDTRDHSGATACMLARQFGHMKIV-ALMETHSPV 166
Cdd:PHA03095  240 VLPLLIAGISINARN-RYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVrAALAKNPSA 316
SAM_Scm-like-3MBT3,4 cd09582
SAM domain of Scm-like-3MBT3,4 proteins of Polycomb group; SAM (sterile alpha motif) domain of ...
 376-424 9.45e-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: 9.45e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1720387813 376 GCLKYLQVFEEQDIDLRIFLTLTESDLKEI-GITLfGPKRKMTSAIARWH 424
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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