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Conserved domains on  [gi|62739181|ref|NP_001015056|]
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rhotekin isoform c [Homo sapiens]

Protein Classification

Anillin and PH_rhotekin2 domain-containing protein( domain architecture ID 10209943)

protein containing domains HR1, Anillin, and PH_rhotekin2

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PH_rhotekin2 cd13249
Anillin Pleckstrin homology (PH) domain; Anillin (Rhotekin/RTKN; also called PLEKHK/Pleckstrin ...
 259-369 4.61e-52

Anillin Pleckstrin homology (PH) domain; Anillin (Rhotekin/RTKN; also called PLEKHK/Pleckstrin homology domain-containing family K) is an actin binding protein involved in cytokinesis. It interacts with GTP-bound Rho proteins and results in the inhibition of their GTPase activity. Dysregulation of the Rho signal transduction pathway has been implicated in many forms of cancer. Anillin proteins have a N-terminal HRI domain/ACC (anti-parallel coiled-coil) finger domain or Rho-binding domain binds small GTPases from the Rho family. The C-terminal PH domain helps target anillin to ectopic septin containing foci. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


:

Pssm-ID: 270069  Cd Length: 111  Bit Score: 172.18  E-value: 4.61e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62739181 259 QPTASGTLRVQQAGE-MQNWAQVHGVLKGTNLFCYRQPEDADTGEEPLLTIAVNKETRVRAGELDQAlGRPFTLSISNQY 337
Cdd:cd13249   1 QEMMSGYLSQQQSVEgLQSWTRLYCVLKGGNLLCYYSPEEIEAKVEPLLTIPINKETRIRAVEKDSK-GRASSLSIINPY 79

                        90       100       110
                ....*....|....*....|....*....|..
gi 62739181 338 GDDEVTHTLQTESREALQSWMEALWQLFFDMS 369
Cdd:cd13249  80 SGEEVTHVLSADSREELQKWMEALWQHFYDMS 111
Anillin pfam08174
Cell division protein anillin; Anillin is a protein involved in septin organization during ...
 67-220 6.86e-41

Cell division protein anillin; Anillin is a protein involved in septin organization during cell division. It is an actin binding protein that is localized to the cleavage furrow, and it maintains the localization of active myosin, which ensures the spatial control of concerted contraction during cytokinesis.


:

Pssm-ID: 462393  Cd Length: 139  Bit Score: 143.57  E-value: 6.86e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62739181    67 CRGRVCISDLRIPLMWKDTEYFKNKGDLHRWAVFLLLQLGEHIQDTEMI-LVDRT-LTDISFQSNVLFAEAGPDFELRLE 144
Cdd:pfam08174   1 CKGKVTISDIRIPLKWRFVDHFKNKGESRRYAFFCLLKCGTEIEATDLVsTLDRTdGTDICFGDPITFSNVPPDFEITVE 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 62739181   145 LYGACV-EEEGALTGGPKRLATKlssslgrssgrrvrasldSAGGSGSSPILLPTPVVGGPRYHLLAHTTLTLAAVQ 220
Cdd:pfam08174  81 VYSLRVtEEKLSSALTPKKLASK------------------LASKSLGRSPGGKLAVRRGSKFKLLGSLTLTLLSVG 139
HR1 super family cl00087
Protein kinase C-related kinase homology region 1 (HR1) domain that binds Rho family small ...
 1-41 1.06e-05

Protein kinase C-related kinase homology region 1 (HR1) domain that binds Rho family small GTPases; The HR1 domain, also called the ACC (anti-parallel coiled-coil) finger domain or Rho-binding domain binds small GTPases from the Rho family. It is found in Rho effector proteins including PKC-related kinases such as vertebrate PRK1 (or PKN) and yeast PKC1 protein kinases C, as well as in rhophilins and Rho-associated kinase (ROCK). Rho family members function as molecular switches, cycling between inactive and active forms, controlling a variety of cellular processes. HR1 domains may occur in repeat arrangements (PKN contains three HR1 domains), separated by a short linker region.


The actual alignment was detected with superfamily member smart00742:

Pssm-ID: 469609  Cd Length: 57  Bit Score: 42.95  E-value: 1.06e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 62739181      1 MREGACKLLAACSQREQAL-EATKSLLVCNSRILSYMGELQR 41
Cdd:smart00742  16 VKEGAENMRKLTSNDRKVLsEAQSMLRESNQKLDLLKEELEK 57
 
Name Accession Description Interval E-value
PH_rhotekin2 cd13249
Anillin Pleckstrin homology (PH) domain; Anillin (Rhotekin/RTKN; also called PLEKHK/Pleckstrin ...
 259-369 4.61e-52

Anillin Pleckstrin homology (PH) domain; Anillin (Rhotekin/RTKN; also called PLEKHK/Pleckstrin homology domain-containing family K) is an actin binding protein involved in cytokinesis. It interacts with GTP-bound Rho proteins and results in the inhibition of their GTPase activity. Dysregulation of the Rho signal transduction pathway has been implicated in many forms of cancer. Anillin proteins have a N-terminal HRI domain/ACC (anti-parallel coiled-coil) finger domain or Rho-binding domain binds small GTPases from the Rho family. The C-terminal PH domain helps target anillin to ectopic septin containing foci. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270069  Cd Length: 111  Bit Score: 172.18  E-value: 4.61e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62739181 259 QPTASGTLRVQQAGE-MQNWAQVHGVLKGTNLFCYRQPEDADTGEEPLLTIAVNKETRVRAGELDQAlGRPFTLSISNQY 337
Cdd:cd13249   1 QEMMSGYLSQQQSVEgLQSWTRLYCVLKGGNLLCYYSPEEIEAKVEPLLTIPINKETRIRAVEKDSK-GRASSLSIINPY 79

                        90       100       110
                ....*....|....*....|....*....|..
gi 62739181 338 GDDEVTHTLQTESREALQSWMEALWQLFFDMS 369
Cdd:cd13249  80 SGEEVTHVLSADSREELQKWMEALWQHFYDMS 111
Anillin pfam08174
Cell division protein anillin; Anillin is a protein involved in septin organization during ...
 67-220 6.86e-41

Cell division protein anillin; Anillin is a protein involved in septin organization during cell division. It is an actin binding protein that is localized to the cleavage furrow, and it maintains the localization of active myosin, which ensures the spatial control of concerted contraction during cytokinesis.


Pssm-ID: 462393  Cd Length: 139  Bit Score: 143.57  E-value: 6.86e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62739181    67 CRGRVCISDLRIPLMWKDTEYFKNKGDLHRWAVFLLLQLGEHIQDTEMI-LVDRT-LTDISFQSNVLFAEAGPDFELRLE 144
Cdd:pfam08174   1 CKGKVTISDIRIPLKWRFVDHFKNKGESRRYAFFCLLKCGTEIEATDLVsTLDRTdGTDICFGDPITFSNVPPDFEITVE 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 62739181   145 LYGACV-EEEGALTGGPKRLATKlssslgrssgrrvrasldSAGGSGSSPILLPTPVVGGPRYHLLAHTTLTLAAVQ 220
Cdd:pfam08174  81 VYSLRVtEEKLSSALTPKKLASK------------------LASKSLGRSPGGKLAVRRGSKFKLLGSLTLTLLSVG 139
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 263-361 1.86e-09

Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.


Pssm-ID: 214574 [Multi-domain]  Cd Length: 102  Bit Score: 54.86  E-value: 1.86e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62739181    263 SGTLRVQQAGEMQNWAQVHGVLKGTNLFCYRQpEDADTGEEPLLTIAVnKETRVRAGELDQALGRPFTLSISNqygDDEV 342
Cdd:smart00233   4 EGWLYKKSGGGKKSWKKRYFVLFNSTLLYYKS-KKDKKSYKPKGSIDL-SGCTVREAPDPDSSKKPHCFEIKT---SDRK 78

                           90
                   ....*....|....*....
gi 62739181    343 THTLQTESREALQSWMEAL 361
Cdd:smart00233  79 TLLLQAESEEEREKWVEAL 97
PH pfam00169
PH domain; PH stands for pleckstrin homology.
 263-361 6.21e-08

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 50.64  E-value: 6.21e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62739181   263 SGTLRVQQAGEMQNWAQVHGVLKGTNLFCYRqPEDADTGEEPLLTIAVNKETRVRAGELDQAlGRPFTLSISNQYGDDEV 342
Cdd:pfam00169   4 EGWLLKKGGGKKKSWKKRYFVLFDGSLLYYK-DDKSGKSKEPKGSISLSGCEVVEVVASDSP-KRKFCFELRTGERTGKR 81

                          90
                  ....*....|....*....
gi 62739181   343 THTLQTESREALQSWMEAL 361
Cdd:pfam00169  82 TYLLQAESEEERKDWIKAI 100
Hr1 smart00742
Rho effector or protein kinase C-related kinase homology region 1 homologues; Alpha-helical ...
 1-41 1.06e-05

Rho effector or protein kinase C-related kinase homology region 1 homologues; Alpha-helical domain found in vertebrate PRK1 and yeast PKC1 protein kinases C. The HR1 in rhophilin bind RhoGTP; those in PRK1 bind RhoA and RhoB. Also called RBD - Rho-binding domain


Pssm-ID: 128981  Cd Length: 57  Bit Score: 42.95  E-value: 1.06e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 62739181      1 MREGACKLLAACSQREQAL-EATKSLLVCNSRILSYMGELQR 41
Cdd:smart00742  16 VKEGAENMRKLTSNDRKVLsEAQSMLRESNQKLDLLKEELEK 57
 
Name Accession Description Interval E-value
PH_rhotekin2 cd13249
Anillin Pleckstrin homology (PH) domain; Anillin (Rhotekin/RTKN; also called PLEKHK/Pleckstrin ...
 259-369 4.61e-52

Anillin Pleckstrin homology (PH) domain; Anillin (Rhotekin/RTKN; also called PLEKHK/Pleckstrin homology domain-containing family K) is an actin binding protein involved in cytokinesis. It interacts with GTP-bound Rho proteins and results in the inhibition of their GTPase activity. Dysregulation of the Rho signal transduction pathway has been implicated in many forms of cancer. Anillin proteins have a N-terminal HRI domain/ACC (anti-parallel coiled-coil) finger domain or Rho-binding domain binds small GTPases from the Rho family. The C-terminal PH domain helps target anillin to ectopic septin containing foci. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270069  Cd Length: 111  Bit Score: 172.18  E-value: 4.61e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62739181 259 QPTASGTLRVQQAGE-MQNWAQVHGVLKGTNLFCYRQPEDADTGEEPLLTIAVNKETRVRAGELDQAlGRPFTLSISNQY 337
Cdd:cd13249   1 QEMMSGYLSQQQSVEgLQSWTRLYCVLKGGNLLCYYSPEEIEAKVEPLLTIPINKETRIRAVEKDSK-GRASSLSIINPY 79

                        90       100       110
                ....*....|....*....|....*....|..
gi 62739181 338 GDDEVTHTLQTESREALQSWMEALWQLFFDMS 369
Cdd:cd13249  80 SGEEVTHVLSADSREELQKWMEALWQHFYDMS 111
Anillin pfam08174
Cell division protein anillin; Anillin is a protein involved in septin organization during ...
 67-220 6.86e-41

Cell division protein anillin; Anillin is a protein involved in septin organization during cell division. It is an actin binding protein that is localized to the cleavage furrow, and it maintains the localization of active myosin, which ensures the spatial control of concerted contraction during cytokinesis.


Pssm-ID: 462393  Cd Length: 139  Bit Score: 143.57  E-value: 6.86e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62739181    67 CRGRVCISDLRIPLMWKDTEYFKNKGDLHRWAVFLLLQLGEHIQDTEMI-LVDRT-LTDISFQSNVLFAEAGPDFELRLE 144
Cdd:pfam08174   1 CKGKVTISDIRIPLKWRFVDHFKNKGESRRYAFFCLLKCGTEIEATDLVsTLDRTdGTDICFGDPITFSNVPPDFEITVE 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 62739181   145 LYGACV-EEEGALTGGPKRLATKlssslgrssgrrvrasldSAGGSGSSPILLPTPVVGGPRYHLLAHTTLTLAAVQ 220
Cdd:pfam08174  81 VYSLRVtEEKLSSALTPKKLASK------------------LASKSLGRSPGGKLAVRRGSKFKLLGSLTLTLLSVG 139
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 263-361 1.86e-09

Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.


Pssm-ID: 214574 [Multi-domain]  Cd Length: 102  Bit Score: 54.86  E-value: 1.86e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62739181    263 SGTLRVQQAGEMQNWAQVHGVLKGTNLFCYRQpEDADTGEEPLLTIAVnKETRVRAGELDQALGRPFTLSISNqygDDEV 342
Cdd:smart00233   4 EGWLYKKSGGGKKSWKKRYFVLFNSTLLYYKS-KKDKKSYKPKGSIDL-SGCTVREAPDPDSSKKPHCFEIKT---SDRK 78

                           90
                   ....*....|....*....
gi 62739181    343 THTLQTESREALQSWMEAL 361
Cdd:smart00233  79 TLLLQAESEEEREKWVEAL 97
PH cd00821
Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are ...
 263-361 2.10e-08

Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 275388 [Multi-domain]  Cd Length: 92  Bit Score: 51.77  E-value: 2.10e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62739181 263 SGTLRVQQAGEMQNWAQVHGVLKGTNLFCYRQPEDAdtGEEPLLTIAVNKETRVRageLDQALGRPFTLSISNqygDDEV 342
Cdd:cd00821   2 EGYLLKRGGGGLKSWKKRWFVLFEGVLLYYKSKKDS--SYKPKGSIPLSGILEVE---EVSPKERPHCFELVT---PDGR 73

                        90
                ....*....|....*....
gi 62739181 343 THTLQTESREALQSWMEAL 361
Cdd:cd00821  74 TYYLQADSEEERQEWLKAL 92
PH pfam00169
PH domain; PH stands for pleckstrin homology.
 263-361 6.21e-08

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 50.64  E-value: 6.21e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62739181   263 SGTLRVQQAGEMQNWAQVHGVLKGTNLFCYRqPEDADTGEEPLLTIAVNKETRVRAGELDQAlGRPFTLSISNQYGDDEV 342
Cdd:pfam00169   4 EGWLLKKGGGKKKSWKKRYFVLFDGSLLYYK-DDKSGKSKEPKGSISLSGCEVVEVVASDSP-KRKFCFELRTGERTGKR 81

                          90
                  ....*....|....*....
gi 62739181   343 THTLQTESREALQSWMEAL 361
Cdd:pfam00169  82 TYLLQAESEEERKDWIKAI 100
Hr1 smart00742
Rho effector or protein kinase C-related kinase homology region 1 homologues; Alpha-helical ...
 1-41 1.06e-05

Rho effector or protein kinase C-related kinase homology region 1 homologues; Alpha-helical domain found in vertebrate PRK1 and yeast PKC1 protein kinases C. The HR1 in rhophilin bind RhoGTP; those in PRK1 bind RhoA and RhoB. Also called RBD - Rho-binding domain


Pssm-ID: 128981  Cd Length: 57  Bit Score: 42.95  E-value: 1.06e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 62739181      1 MREGACKLLAACSQREQAL-EATKSLLVCNSRILSYMGELQR 41
Cdd:smart00742  16 VKEGAENMRKLTSNDRKVLsEAQSMLRESNQKLDLLKEELEK 57
PH_anillin cd01263
Anillin Pleckstrin homology (PH) domain; Anillin (Rhotekin/RTKN; also called PLEKHK/Pleckstrin ...
 262-361 1.28e-03

Anillin Pleckstrin homology (PH) domain; Anillin (Rhotekin/RTKN; also called PLEKHK/Pleckstrin homology domain-containing family K) is an actin binding protein involved in cytokinesis. It interacts with GTP-bound Rho proteins and results in the inhibition of their GTPase activity. Dysregulation of the Rho signal transduction pathway has been implicated in many forms of cancer. Anillin proteins have a N-terminal HRI domain/ACC (anti-parallel coiled-coil) finger domain or Rho-binding domain binds small GTPases from the Rho family. The C-terminal PH domain helps target anillin to ectopic septin containing foci. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 269964  Cd Length: 121  Bit Score: 38.80  E-value: 1.28e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62739181 262 ASGTLRVQQ-AGEMQNWAQVHGVLKGTNLFCYRQPEDADTgEEPLLTIAVNKETRVRAGELDQAL-GRPFTL----SISN 335
Cdd:cd01263   4 YRGFLTVFEdVSGLGAWHRRWCVLRGGYLSFWKYPDDEEK-KKPIGSIDLTKCITEKVEPAPRELcARPNTFlletLRPA 82

                        90       100       110
                ....*....|....*....|....*....|.
gi 62739181 336 QYGDDEVT-----HTLQTESREALQSWMEAL 361
Cdd:cd01263  83 EDDDRDDTnekirVLLSADTKEERIEWLSAL 113
PH_Ses cd13288
Sesquipedalian family Pleckstrin homology (PH) domain; The sesquipedalian family has 2 ...
 283-368 2.67e-03

Sesquipedalian family Pleckstrin homology (PH) domain; The sesquipedalian family has 2 mammalian members: Ses1 and Ses2, which are also callled 7 kDa inositol polyphosphate phosphatase-interacting protein 1 and 2. They play a role in endocytic trafficking and are required for receptor recycling from endosomes, both to the trans-Golgi network and the plasma membrane. Members of this family form homodimers and heterodimers. Sesquipedalian interacts with inositol polyphosphate 5-phosphatase OCRL-1 (INPP5F) also known as Lowe oculocerebrorenal syndrome protein, a phosphatase enzyme that is involved in actin polymerization and is found in the trans-Golgi network and INPP5B. Sesquipedalian contains a single PH domain. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270105 [Multi-domain]  Cd Length: 120  Bit Score: 37.99  E-value: 2.67e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62739181 283 VLKGTNLFCYRQPEDadtgEEPLLTIaVNKETRVRAGELDQalgrPFTLSISNQyGDDEVTHTLQTESREALQSWMEALW 362
Cdd:cd13288  30 VLKGNLLFYFEKKGD----REPLGVI-VLEGCTVELAEDAE----PYAFAIRFD-GPGARSYVLAAENQEDMESWMKALS 99


                ....*.
gi 62739181 363 QLFFDM 368
Cdd:cd13288 100 RASYDY 105
 
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.
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