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Conserved domains on  [gi|2217330057|ref|XP_047301347|]
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rhotekin isoform X2 [Homo sapiens]

Protein Classification

Anillin and PH_rhotekin2 domain-containing protein( domain architecture ID 10654330)

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 ...
 296-406 3.24e-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: 171.80  E-value: 3.24e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330057 296 QPTASGTLRVQQAGE-MQNWAQVHGVLKGTNLFCYRQPEDADTGEEPLLTIAVNKETRVRAGELDQAlGRPFTLSISNQY 374
Cdd:cd13249     1 QEMMSGYLSQQQSVEgLQSWTRLYCVLKGGNLLCYYSPEEIEAKVEPLLTIPINKETRIRAVEKDSK-GRASSLSIINPY 79

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2217330057 375 GDDEVTHTLQTESREALQSWMEALWQLFFDMS 406
Cdd:cd13249    80 SGEEVTHVLSADSREELQKWMEALWQHFYDMS 111
Anillin pfam08174
Cell division protein anillin; Anillin is a protein involved in septin organization during ...
 104-257 3.91e-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: 3.91e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330057 104 CRGRVCISDLRIPLMWKDTEYFKNKGDLHRWAVFLLLQLGEHIQDTEMI-LVDRT-LTDISFQSNVLFAEAGPDFELRLE 181
Cdd:pfam08174   1 CKGKVTISDIRIPLKWRFVDHFKNKGESRRYAFFCLLKCGTEIEATDLVsTLDRTdGTDICFGDPITFSNVPPDFEITVE 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217330057 182 LYGACV-EEEGALTGGPKRLATKlssslgrssgrrvrasldSAGGSGSSPILLPTPVVGGPRYHLLAHTTLTLAAVQ 257
Cdd:pfam08174  81 VYSLRVtEEKLSSALTPKKLASK------------------LASKSLGRSPGGKLAVRRGSKFKLLGSLTLTLLSVG 139
Hr1 smart00742
Rho effector or protein kinase C-related kinase homology region 1 homologues; Alpha-helical ...
 23-78 4.57e-11

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: 57.97  E-value: 4.57e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2217330057   23 LEDTELQRKLDHEIRMREGACKLLAACSQREQAL-EATKSLLVCNSRILSYMGELQR 78
Cdd:smart00742   1 LRLEDLRRKIEKELKVKEGAENMRKLTSNDRKVLsEAQSMLRESNQKLDLLKEELEK 57
 
Name Accession Description Interval E-value
PH_rhotekin2 cd13249
Anillin Pleckstrin homology (PH) domain; Anillin (Rhotekin/RTKN; also called PLEKHK/Pleckstrin ...
 296-406 3.24e-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: 171.80  E-value: 3.24e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330057 296 QPTASGTLRVQQAGE-MQNWAQVHGVLKGTNLFCYRQPEDADTGEEPLLTIAVNKETRVRAGELDQAlGRPFTLSISNQY 374
Cdd:cd13249     1 QEMMSGYLSQQQSVEgLQSWTRLYCVLKGGNLLCYYSPEEIEAKVEPLLTIPINKETRIRAVEKDSK-GRASSLSIINPY 79

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2217330057 375 GDDEVTHTLQTESREALQSWMEALWQLFFDMS 406
Cdd:cd13249    80 SGEEVTHVLSADSREELQKWMEALWQHFYDMS 111
Anillin pfam08174
Cell division protein anillin; Anillin is a protein involved in septin organization during ...
 104-257 3.91e-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: 3.91e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330057 104 CRGRVCISDLRIPLMWKDTEYFKNKGDLHRWAVFLLLQLGEHIQDTEMI-LVDRT-LTDISFQSNVLFAEAGPDFELRLE 181
Cdd:pfam08174   1 CKGKVTISDIRIPLKWRFVDHFKNKGESRRYAFFCLLKCGTEIEATDLVsTLDRTdGTDICFGDPITFSNVPPDFEITVE 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217330057 182 LYGACV-EEEGALTGGPKRLATKlssslgrssgrrvrasldSAGGSGSSPILLPTPVVGGPRYHLLAHTTLTLAAVQ 257
Cdd:pfam08174  81 VYSLRVtEEKLSSALTPKKLASK------------------LASKSLGRSPGGKLAVRRGSKFKLLGSLTLTLLSVG 139
Hr1 smart00742
Rho effector or protein kinase C-related kinase homology region 1 homologues; Alpha-helical ...
 23-78 4.57e-11

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: 57.97  E-value: 4.57e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2217330057   23 LEDTELQRKLDHEIRMREGACKLLAACSQREQAL-EATKSLLVCNSRILSYMGELQR 78
Cdd:smart00742   1 LRLEDLRRKIEKELKVKEGAENMRKLTSNDRKVLsEAQSMLRESNQKLDLLKEELEK 57
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 300-398 1.72e-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: 1.72e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330057  300 SGTLRVQQAGEMQNWAQVHGVLKGTNLFCYRQpEDADTGEEPLLTIAVnKETRVRAGELDQALGRPFTLSISNqygDDEV 379
Cdd:smart00233   4 EGWLYKKSGGGKKSWKKRYFVLFNSTLLYYKS-KKDKKSYKPKGSIDL-SGCTVREAPDPDSSKKPHCFEIKT---SDRK 78

                           90
                   ....*....|....*....
gi 2217330057  380 THTLQTESREALQSWMEAL 398
Cdd:smart00233  79 TLLLQAESEEEREKWVEAL 97
PH pfam00169
PH domain; PH stands for pleckstrin homology.
 300-398 5.73e-08

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 50.64  E-value: 5.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330057 300 SGTLRVQQAGEMQNWAQVHGVLKGTNLFCYRqPEDADTGEEPLLTIAVNKETRVRAGELDQAlGRPFTLSISNQYGDDEV 379
Cdd:pfam00169   4 EGWLLKKGGGKKKSWKKRYFVLFDGSLLYYK-DDKSGKSKEPKGSISLSGCEVVEVVASDSP-KRKFCFELRTGERTGKR 81

                          90
                  ....*....|....*....
gi 2217330057 380 THTLQTESREALQSWMEAL 398
Cdd:pfam00169  82 TYLLQAESEEERKDWIKAI 100
HR1 pfam02185
Hr1 repeat; The HR1 repeat was first described as a three times repeated homology region of ...
 26-83 1.00e-02

Hr1 repeat; The HR1 repeat was first described as a three times repeated homology region of the N-terminal non-catalytic part of protein kinase PRK1(PKN). The first two of these repeats were later shown to bind the small G protein rho known to activate PKN in its GTP-bound form. Similar rho-binding domains also occur in a number of other protein kinases and in the rho-binding proteins rhophilin and rhotekin. Recently, the structure of the N-terminal HR1 repeat complexed with RhoA has been determined by X-ray crystallography. It forms an antiparallel coiled-coil fold termed an ACC finger.


Pssm-ID: 460478 [Multi-domain]  Cd Length: 67  Bit Score: 34.80  E-value: 1.00e-02
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217330057  26 TELQRKLDHEIRMREGACKLLAACSQREQ--ALEATKSLLVCNSRILSY----MGELQRRKEAQ 83
Cdd:pfam02185   3 QELRKKIEVEKKIKEGAENMLRLLQATKDrkVLAEAESELRESNRKIQLlreqLRELQARHLPS 66
 
Name Accession Description Interval E-value
PH_rhotekin2 cd13249
Anillin Pleckstrin homology (PH) domain; Anillin (Rhotekin/RTKN; also called PLEKHK/Pleckstrin ...
 296-406 3.24e-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: 171.80  E-value: 3.24e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330057 296 QPTASGTLRVQQAGE-MQNWAQVHGVLKGTNLFCYRQPEDADTGEEPLLTIAVNKETRVRAGELDQAlGRPFTLSISNQY 374
Cdd:cd13249     1 QEMMSGYLSQQQSVEgLQSWTRLYCVLKGGNLLCYYSPEEIEAKVEPLLTIPINKETRIRAVEKDSK-GRASSLSIINPY 79

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2217330057 375 GDDEVTHTLQTESREALQSWMEALWQLFFDMS 406
Cdd:cd13249    80 SGEEVTHVLSADSREELQKWMEALWQHFYDMS 111
Anillin pfam08174
Cell division protein anillin; Anillin is a protein involved in septin organization during ...
 104-257 3.91e-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: 3.91e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330057 104 CRGRVCISDLRIPLMWKDTEYFKNKGDLHRWAVFLLLQLGEHIQDTEMI-LVDRT-LTDISFQSNVLFAEAGPDFELRLE 181
Cdd:pfam08174   1 CKGKVTISDIRIPLKWRFVDHFKNKGESRRYAFFCLLKCGTEIEATDLVsTLDRTdGTDICFGDPITFSNVPPDFEITVE 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217330057 182 LYGACV-EEEGALTGGPKRLATKlssslgrssgrrvrasldSAGGSGSSPILLPTPVVGGPRYHLLAHTTLTLAAVQ 257
Cdd:pfam08174  81 VYSLRVtEEKLSSALTPKKLASK------------------LASKSLGRSPGGKLAVRRGSKFKLLGSLTLTLLSVG 139
Hr1 smart00742
Rho effector or protein kinase C-related kinase homology region 1 homologues; Alpha-helical ...
 23-78 4.57e-11

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: 57.97  E-value: 4.57e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2217330057   23 LEDTELQRKLDHEIRMREGACKLLAACSQREQAL-EATKSLLVCNSRILSYMGELQR 78
Cdd:smart00742   1 LRLEDLRRKIEKELKVKEGAENMRKLTSNDRKVLsEAQSMLRESNQKLDLLKEELEK 57
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 300-398 1.72e-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: 1.72e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330057  300 SGTLRVQQAGEMQNWAQVHGVLKGTNLFCYRQpEDADTGEEPLLTIAVnKETRVRAGELDQALGRPFTLSISNqygDDEV 379
Cdd:smart00233   4 EGWLYKKSGGGKKSWKKRYFVLFNSTLLYYKS-KKDKKSYKPKGSIDL-SGCTVREAPDPDSSKKPHCFEIKT---SDRK 78

                           90
                   ....*....|....*....
gi 2217330057  380 THTLQTESREALQSWMEAL 398
Cdd:smart00233  79 TLLLQAESEEEREKWVEAL 97
PH cd00821
Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are ...
 300-398 1.94e-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: 1.94e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330057 300 SGTLRVQQAGEMQNWAQVHGVLKGTNLFCYRQPEDAdtGEEPLLTIAVNKETRVRageLDQALGRPFTLSISNqygDDEV 379
Cdd:cd00821     2 EGYLLKRGGGGLKSWKKRWFVLFEGVLLYYKSKKDS--SYKPKGSIPLSGILEVE---EVSPKERPHCFELVT---PDGR 73

                          90
                  ....*....|....*....
gi 2217330057 380 THTLQTESREALQSWMEAL 398
Cdd:cd00821    74 TYYLQADSEEERQEWLKAL 92
PH pfam00169
PH domain; PH stands for pleckstrin homology.
 300-398 5.73e-08

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 50.64  E-value: 5.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330057 300 SGTLRVQQAGEMQNWAQVHGVLKGTNLFCYRqPEDADTGEEPLLTIAVNKETRVRAGELDQAlGRPFTLSISNQYGDDEV 379
Cdd:pfam00169   4 EGWLLKKGGGKKKSWKKRYFVLFDGSLLYYK-DDKSGKSKEPKGSISLSGCEVVEVVASDSP-KRKFCFELRTGERTGKR 81

                          90
                  ....*....|....*....
gi 2217330057 380 THTLQTESREALQSWMEAL 398
Cdd:pfam00169  82 TYLLQAESEEERKDWIKAI 100
PH_anillin cd01263
Anillin Pleckstrin homology (PH) domain; Anillin (Rhotekin/RTKN; also called PLEKHK/Pleckstrin ...
 299-398 9.19e-04

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: 39.18  E-value: 9.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330057 299 ASGTLRVQQ-AGEMQNWAQVHGVLKGTNLFCYRQPEDADTgEEPLLTIAVNKETRVRAGELDQAL-GRPFTL----SISN 372
Cdd:cd01263     4 YRGFLTVFEdVSGLGAWHRRWCVLRGGYLSFWKYPDDEEK-KKPIGSIDLTKCITEKVEPAPRELcARPNTFlletLRPA 82

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2217330057 373 QYGDDEVT-----HTLQTESREALQSWMEAL 398
Cdd:cd01263    83 EDDDRDDTnekirVLLSADTKEERIEWLSAL 113
PH_Ses cd13288
Sesquipedalian family Pleckstrin homology (PH) domain; The sesquipedalian family has 2 ...
 320-405 4.55e-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: 37.22  E-value: 4.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330057 320 VLKGTNLFCYRQPEDadtgEEPLLTIaVNKETRVRAGELDQalgrPFTLSISNQyGDDEVTHTLQTESREALQSWMEALW 399
Cdd:cd13288    30 VLKGNLLFYFEKKGD----REPLGVI-VLEGCTVELAEDAE----PYAFAIRFD-GPGARSYVLAAENQEDMESWMKALS 99


                  ....*.
gi 2217330057 400 QLFFDM 405
Cdd:cd13288   100 RASYDY 105
PH_PEPP1_2_3 cd13248
Phosphoinositol 3-phosphate binding proteins 1, 2, and 3 pleckstrin homology (PH) domain; ...
 297-398 9.65e-03

Phosphoinositol 3-phosphate binding proteins 1, 2, and 3 pleckstrin homology (PH) domain; PEPP1 (also called PLEKHA4/PH domain-containing family A member 4 and RHOXF1/Rhox homeobox family member 1), and related homologs PEPP2 (also called PLEKHA5/PH domain-containing family A member 5) and PEPP3 (also called PLEKHA6/PH domain-containing family A member 6), have PH domains that interact specifically with PtdIns(3,4)P3. Other proteins that bind PtdIns(3,4)P3 specifically are: TAPP1 (tandem PH-domain-containing protein-1) and TAPP2], PtdIns3P AtPH1, and Ptd- Ins(3,5)P2 (centaurin-beta2). All of these proteins contain at least 5 of the 6 conserved amino acids that make up the putative phosphatidylinositol 3,4,5- trisphosphate-binding motif (PPBM) located at their N-terminus. 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: 270068  Cd Length: 104  Bit Score: 35.71  E-value: 9.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330057 297 PTASGTLRVQQAGEMQNWAQVHGVLKGTNLFCYRQPEDadtgEEPLLTIAVNKETRVRAGELDQAlGRPFTLSISNQygd 376
Cdd:cd13248     7 VVMSGWLHKQGGSGLKNWRKRWFVLKDNCLYYYKDPEE----EKALGSILLPSYTISPAPPSDEI-SRKFAFKAEHA--- 78

                          90       100
                  ....*....|....*....|..
gi 2217330057 377 DEVTHTLQTESREALQSWMEAL 398
Cdd:cd13248    79 NMRTYYFAADTAEEMEQWMNAM 100
HR1 pfam02185
Hr1 repeat; The HR1 repeat was first described as a three times repeated homology region of ...
 26-83 1.00e-02

Hr1 repeat; The HR1 repeat was first described as a three times repeated homology region of the N-terminal non-catalytic part of protein kinase PRK1(PKN). The first two of these repeats were later shown to bind the small G protein rho known to activate PKN in its GTP-bound form. Similar rho-binding domains also occur in a number of other protein kinases and in the rho-binding proteins rhophilin and rhotekin. Recently, the structure of the N-terminal HR1 repeat complexed with RhoA has been determined by X-ray crystallography. It forms an antiparallel coiled-coil fold termed an ACC finger.


Pssm-ID: 460478 [Multi-domain]  Cd Length: 67  Bit Score: 34.80  E-value: 1.00e-02
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217330057  26 TELQRKLDHEIRMREGACKLLAACSQREQ--ALEATKSLLVCNSRILSY----MGELQRRKEAQ 83
Cdd:pfam02185   3 QELRKKIEVEKKIKEGAENMLRLLQATKDrkVLAEAESELRESNRKIQLlreqLRELQARHLPS 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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