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Conserved domains on  [gi|2024415360|ref|XP_040558296|]
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rhotekin-2 isoform X1 [Gallus gallus]

Protein Classification

RTKN2 family PH domain-containing protein; PH domain-containing protein( domain architecture ID 10209943)

RTKN2 family PH (pleckstrin homology) domain-containing protein similar to PH region of rhotekin-2 (RTKN2) that may play an important role in lymphopoiesis| PH (pleckstrin homology) domain-containing protein similar to Caenorhabditis elegans protein C15H7.4

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 ...
 284-421 1.14e-60

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: 197.61  E-value: 1.14e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024415360 284 RDMMAGFLNQQQMIGNLTSWRRLYCVLRGGKLFCYYSPEEIEAEVEPALTVSINkgkrdllydcsipcsplatfweafvl 363
Cdd:cd13249     1 QEMMSGYLSQQQSVEGLQSWTRLYCVLKGGNLLCYYSPEEIEAKVEPLLTIPIN-------------------------- 54

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2024415360 364 sKETRIRSVDKDSKRRTNNFSVINPVSGEAATQLFATDSREELHKWMEAFWQHFYDLS 421
Cdd:cd13249    55 -KETRIRAVEKDSKGRASSLSIINPYSGEEVTHVLSADSREELQKWMEALWQHFYDMS 111
Anillin pfam08174
Cell division protein anillin; Anillin is a protein involved in septin organization during ...
 95-245 4.19e-50

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: 170.53  E-value: 4.19e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024415360  95 CRAKVALSDIRIPLMWKGSDHFNNKENSQRYAVFCLFRMGAEVFDTDVA-IVDKA-ITDICFENVTIFDEAGPDFQVKVE 172
Cdd:pfam08174   1 CKGKVTISDIRIPLKWRFVDHFKNKGESRRYAFFCLLKCGTEIEATDLVsTLDRTdGTDICFGDPITFSNVPPDFEITVE 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024415360 173 VYS-CCMEESLYIANTPKKLVKKL-KTSLSKATGKKLKATleddgtdsillsdpdiHGAKYSLLAYTTLGLESAE 245
Cdd:pfam08174  81 VYSlRVTEEKLSSALTPKKLASKLaSKSLGRSPGGKLAVR----------------RGSKFKLLGSLTLTLLSVG 139
HR1 super family cl00087
Protein kinase C-related kinase homology region 1 (HR1) domain that binds Rho family small ...
 19-69 9.06e-07

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: 46.03  E-value: 9.06e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2024415360   19 NIQEKMDFEIRIREGIRKLLTVSTQKDQLLQAV-KNLMVCNARIHAYRTELQ 69
Cdd:smart00742   5 DLRRKIEKELKVKEGAENMRKLTSNDRKVLSEAqSMLRESNQKLDLLKEELE 56
 
Name Accession Description Interval E-value
PH_rhotekin2 cd13249
Anillin Pleckstrin homology (PH) domain; Anillin (Rhotekin/RTKN; also called PLEKHK/Pleckstrin ...
 284-421 1.14e-60

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: 197.61  E-value: 1.14e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024415360 284 RDMMAGFLNQQQMIGNLTSWRRLYCVLRGGKLFCYYSPEEIEAEVEPALTVSINkgkrdllydcsipcsplatfweafvl 363
Cdd:cd13249     1 QEMMSGYLSQQQSVEGLQSWTRLYCVLKGGNLLCYYSPEEIEAKVEPLLTIPIN-------------------------- 54

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2024415360 364 sKETRIRSVDKDSKRRTNNFSVINPVSGEAATQLFATDSREELHKWMEAFWQHFYDLS 421
Cdd:cd13249    55 -KETRIRAVEKDSKGRASSLSIINPYSGEEVTHVLSADSREELQKWMEALWQHFYDMS 111
Anillin pfam08174
Cell division protein anillin; Anillin is a protein involved in septin organization during ...
 95-245 4.19e-50

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: 170.53  E-value: 4.19e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024415360  95 CRAKVALSDIRIPLMWKGSDHFNNKENSQRYAVFCLFRMGAEVFDTDVA-IVDKA-ITDICFENVTIFDEAGPDFQVKVE 172
Cdd:pfam08174   1 CKGKVTISDIRIPLKWRFVDHFKNKGESRRYAFFCLLKCGTEIEATDLVsTLDRTdGTDICFGDPITFSNVPPDFEITVE 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024415360 173 VYS-CCMEESLYIANTPKKLVKKL-KTSLSKATGKKLKATleddgtdsillsdpdiHGAKYSLLAYTTLGLESAE 245
Cdd:pfam08174  81 VYSlRVTEEKLSSALTPKKLASKLaSKSLGRSPGGKLAVR----------------RGSKFKLLGSLTLTLLSVG 139
Hr1 smart00742
Rho effector or protein kinase C-related kinase homology region 1 homologues; Alpha-helical ...
 19-69 9.06e-07

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: 46.03  E-value: 9.06e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2024415360   19 NIQEKMDFEIRIREGIRKLLTVSTQKDQLLQAV-KNLMVCNARIHAYRTELQ 69
Cdd:smart00742   5 DLRRKIEKELKVKEGAENMRKLTSNDRKVLSEAqSMLRESNQKLDLLKEELE 56
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 287-413 3.12e-06

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: 46.00  E-value: 3.12e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024415360  287 MAGFLNQQQMIGNlTSWRRLYCVLRGGKLfCYYSPEEIEAEVEPALTVSINkgkrdllyDCSIpcsplatfweafvlske 366
Cdd:smart00233   3 KEGWLYKKSGGGK-KSWKKRYFVLFNSTL-LYYKSKKDKKSYKPKGSIDLS--------GCTV----------------- 55

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 2024415360  367 trIRSVDKDSKRRTNNFSVINPvsgEAATQLFATDSREELHKWMEAF 413
Cdd:smart00233  56 --REAPDPDSSKKPHCFEIKTS---DRKTLLLQAESEEEREKWVEAL 97
PH pfam00169
PH domain; PH stands for pleckstrin homology.
 286-413 1.15e-05

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 44.48  E-value: 1.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024415360 286 MMAGFLNQQQMiGNLTSWRRLYCVLRGGKLFcYYSPEeieaevepaltvsinKGKRDLLYDCSIPcsplatfweafvLSK 365
Cdd:pfam00169   2 VKEGWLLKKGG-GKKKSWKKRYFVLFDGSLL-YYKDD---------------KSGKSKEPKGSIS------------LSG 52

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2024415360 366 ETRIRSVDKDSKRRTNNFSVINPVSGEAATQLFATDSREELHKWMEAF 413
Cdd:pfam00169  53 CEVVEVVASDSPKRKFCFELRTGERTGKRTYLLQAESEEERKDWIKAI 100
 
Name Accession Description Interval E-value
PH_rhotekin2 cd13249
Anillin Pleckstrin homology (PH) domain; Anillin (Rhotekin/RTKN; also called PLEKHK/Pleckstrin ...
 284-421 1.14e-60

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: 197.61  E-value: 1.14e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024415360 284 RDMMAGFLNQQQMIGNLTSWRRLYCVLRGGKLFCYYSPEEIEAEVEPALTVSINkgkrdllydcsipcsplatfweafvl 363
Cdd:cd13249     1 QEMMSGYLSQQQSVEGLQSWTRLYCVLKGGNLLCYYSPEEIEAKVEPLLTIPIN-------------------------- 54

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2024415360 364 sKETRIRSVDKDSKRRTNNFSVINPVSGEAATQLFATDSREELHKWMEAFWQHFYDLS 421
Cdd:cd13249    55 -KETRIRAVEKDSKGRASSLSIINPYSGEEVTHVLSADSREELQKWMEALWQHFYDMS 111
Anillin pfam08174
Cell division protein anillin; Anillin is a protein involved in septin organization during ...
 95-245 4.19e-50

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: 170.53  E-value: 4.19e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024415360  95 CRAKVALSDIRIPLMWKGSDHFNNKENSQRYAVFCLFRMGAEVFDTDVA-IVDKA-ITDICFENVTIFDEAGPDFQVKVE 172
Cdd:pfam08174   1 CKGKVTISDIRIPLKWRFVDHFKNKGESRRYAFFCLLKCGTEIEATDLVsTLDRTdGTDICFGDPITFSNVPPDFEITVE 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024415360 173 VYS-CCMEESLYIANTPKKLVKKL-KTSLSKATGKKLKATleddgtdsillsdpdiHGAKYSLLAYTTLGLESAE 245
Cdd:pfam08174  81 VYSlRVTEEKLSSALTPKKLASKLaSKSLGRSPGGKLAVR----------------RGSKFKLLGSLTLTLLSVG 139
PH_anillin cd01263
Anillin Pleckstrin homology (PH) domain; Anillin (Rhotekin/RTKN; also called PLEKHK/Pleckstrin ...
 287-420 5.15e-11

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: 60.37  E-value: 5.15e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024415360 287 MAGFLNQQQMIGNLTSWRRLYCVLRGGKLFCYYSPEEiEAEVEPALTVSINKgkrdllydcsipCSplatfweafvlskE 366
Cdd:cd01263     4 YRGFLTVFEDVSGLGAWHRRWCVLRGGYLSFWKYPDD-EEKKKPIGSIDLTK------------CI-------------T 57

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024415360 367 TRIRSVDKDSKRRTNNFSVINPVSGEAATQ---------LFATDSREELHKWMEAFWQHFYDL 420
Cdd:cd01263    58 EKVEPAPRELCARPNTFLLETLRPAEDDDRddtnekirvLLSADTKEERIEWLSALNQTLADL 120
PH cd00821
Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are ...
 287-413 4.79e-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: 51.00  E-value: 4.79e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024415360 287 MAGFLNQQQMiGNLTSWRRLYCVLRGGKLFCYYSPEEIEAEvepaltvsinkgkrdllYDCSIPcsplatfweafvLSKE 366
Cdd:cd00821     1 KEGYLLKRGG-GGLKSWKKRWFVLFEGVLLYYKSKKDSSYK-----------------PKGSIP------------LSGI 50

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2024415360 367 TRIRSVDKDSKRRTnnFSVINPVSgeaATQLFATDSREELHKWMEAF 413
Cdd:cd00821    51 LEVEEVSPKERPHC--FELVTPDG---RTYYLQADSEEERQEWLKAL 92
Hr1 smart00742
Rho effector or protein kinase C-related kinase homology region 1 homologues; Alpha-helical ...
 19-69 9.06e-07

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: 46.03  E-value: 9.06e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2024415360   19 NIQEKMDFEIRIREGIRKLLTVSTQKDQLLQAV-KNLMVCNARIHAYRTELQ 69
Cdd:smart00742   5 DLRRKIEKELKVKEGAENMRKLTSNDRKVLSEAqSMLRESNQKLDLLKEELE 56
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 287-413 3.12e-06

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: 46.00  E-value: 3.12e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024415360  287 MAGFLNQQQMIGNlTSWRRLYCVLRGGKLfCYYSPEEIEAEVEPALTVSINkgkrdllyDCSIpcsplatfweafvlske 366
Cdd:smart00233   3 KEGWLYKKSGGGK-KSWKKRYFVLFNSTL-LYYKSKKDKKSYKPKGSIDLS--------GCTV----------------- 55

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 2024415360  367 trIRSVDKDSKRRTNNFSVINPvsgEAATQLFATDSREELHKWMEAF 413
Cdd:smart00233  56 --REAPDPDSSKKPHCFEIKTS---DRKTLLLQAESEEEREKWVEAL 97
PH pfam00169
PH domain; PH stands for pleckstrin homology.
 286-413 1.15e-05

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 44.48  E-value: 1.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024415360 286 MMAGFLNQQQMiGNLTSWRRLYCVLRGGKLFcYYSPEeieaevepaltvsinKGKRDLLYDCSIPcsplatfweafvLSK 365
Cdd:pfam00169   2 VKEGWLLKKGG-GKKKSWKKRYFVLFDGSLL-YYKDD---------------KSGKSKEPKGSIS------------LSG 52

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2024415360 366 ETRIRSVDKDSKRRTNNFSVINPVSGEAATQLFATDSREELHKWMEAF 413
Cdd:pfam00169  53 CEVVEVVASDSPKRKFCFELRTGERTGKRTYLLQAESEEERKDWIKAI 100
PH_PEPP1_2_3 cd13248
Phosphoinositol 3-phosphate binding proteins 1, 2, and 3 pleckstrin homology (PH) domain; ...
 286-412 7.13e-05

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: 42.26  E-value: 7.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024415360 286 MMAGFLNQQQMIGnLTSWRRLYCVLRGGKLFCYYSPEEIEaevepALTvSInkgkrdllydcsipcsPLATFweafvlsk 365
Cdd:cd13248     8 VMSGWLHKQGGSG-LKNWRKRWFVLKDNCLYYYKDPEEEK-----ALG-SI----------------LLPSY-------- 56

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2024415360 366 etRIRSVDKDSKR-RTNNFSVINPvsgEAATQLFATDSREELHKWMEA 412
Cdd:cd13248    57 --TISPAPPSDEIsRKFAFKAEHA---NMRTYYFAADTAEEMEQWMNA 99
 
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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